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Last update 23 Jan 2025

PLOD1

Last update 23 Jan 2025

Basic Info

Synonyms

LH1, LLH, Lysyl hydroxylase 1

+ [3]

Introduction

Part of a complex composed of PLOD1, P3H3 and P3H4 that catalyzes hydroxylation of lysine residues in collagen alpha chains and is required for normal assembly and cross-linkling of collagen fibrils (By similarity). Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens (PubMed:8621606, PubMed:10686424, PubMed:15854030). These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (Probable).

Drugs associated with PLOD1

Kyphoscoliotic EDS(UMass Chan Medical School)

Target

PLOD1

Mechanism

PLOD1 modulators

Active Org.

UMass Chan Medical School

Originator Org.

UMass Chan Medical School

Active Indication

Ehlers-Danlos Syndrome

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with PLOD1

100 Translational Medicine associated with PLOD1

0 Patents (Medical) associated with PLOD1

667

Literatures (Medical) associated with PLOD1

07 Jan 2025·Biochemistry

The Thermal-Stable LH1–RC Complex of a Hot Spring Purple Bacterium Powers Photosynthesis with Extremely Low-Energy Near-Infrared Light

Article

Author: Honda, Mai ; Kimura, Yukihiro ; Hall, Malgorzata ; Takenaka, Shinji ; Mori, Kaisei ; Kishikawa, Jun-ichi ; Mio, Kazuhiro ; Tani, Kazutoshi ; Sasaki, Yuji C. ; Humbel, Bruno M. ; Mizoguchi, Akira ; Purba, Endang R. ; Madigan, Michael T. ; Kanno, Ryo ; Wang-Otomo, Zheng-Yu ; Mochizuki, Toshiaki ; Matsuda, Yoshiki ; Seto, Ryuta ; Mitsuoka, Kaoru ; Ohkubo, Tatsunari ; Mino, Hiroyuki

Blastochloris (Blc.) tepida is a hot spring purple nonsulfur phototrophic bacterium that contains bacteriochlorophyll (BChl) b. Here, we present a 2.21 Å cryo-EM structure of the thermostable light-harvesting 1-reaction center (LH1-RC) complex from Blc. tepida. The LH1 ring comprises 16 circularly arranged αβγ-subunits plus one αβ-subunit that surround the RC complex composed of C-, H-, L-, and M-subunits. In a comparative study, the Blc. tepida LH1-RC showed numerous electrostatic and hydrophobic interactions both within the LH1 complex itself and between the LH1 and the RC complexes that are absent from the LH1-RC complex of its mesophilic counterpart, Blc. viridis. These additional interactions result in a tightly packed LH1-RC architecture with a reduced accessible surface area per volume that enhances the thermal stability of the Blc. tepida complex and allows the light reactions of photosynthesis to proceed at hot spring temperatures. Moreover, based on high-resolution structural information combined with spectroscopic evidence, the unique photosynthetic property of the Blc. tepida LH1-RC─absorption of energy-poor near-infrared light beyond 1000 nm─can be attributed to strong hydrogen-bonding interactions between the C3-acetyl C═O of the LH1 BChl b and two LH1 α-Trp residues, structural rigidity of the LH1, and the enhanced exciton coupling of the LH1 BChls of this thermophile.

01 Jan 2025·Biochimica et Biophysica Acta (BBA) - Bioenergetics

Comparative thermo- and piezostability study of photosynthetic core complexes containing bacteriochlorophyll a or b

Article

Author: Kangur, Liina ; Leiger, Kristjan ; Freiberg, Arvi ; Rätsep, Margus ; Wang-Otomo, Zheng-Yu

The resilience of biological systems to fluctuating environmental conditions is a crucial evolutionary advantage. In this study, we examine the thermo- and piezo-stability of the LH1-RC pigment-protein complex, the simplest photosynthetic unit, in three species of phototropic purple bacteria, each containing only this core complex. Among these species, Blastochloris viridis and Blastochloris tepida utilize bacteriochlorophyll b as the main light-harvesting pigment, while Rhodospirillum rubrum relies on bacteriochlorophyll a. Through spectroscopic analyses, we observed limited reversibility in the effects of temperature and pressure, likely due to the malleability of pigment binding sites within the light-harvesting LH1 complex. In terms of thermal robustness, LH1 complexes in a detergent environment progressively dissociate into dimeric (B820) and monomeric (B777) subunits. However, in the native membrane, degradation primarily occurs directly into B777 without the intermediate formation of B820. Interestingly, while high-pressure compression of core complexes from Blastochloris viridis and Blastochloris tepida caused significant changes in compressibility around 1.3 kbar and the formation of B777 and B820 subunits upon decompression, no such compressibility changes or pressure-induced dissociation were observed in Rhodospirillum rubrum complexes, even at pressures as high as 11 kbar. This study reveals significant differences in the piezo- and thermal properties of phototrophs containing either BChl a or BChl b, underscoring the critical role of structural factors in understanding the temperature- and pressure-induced denaturation phenomena in photosynthetic complexes. Rhodospirillum rubrum, in particular, stands out as one of the most thermodynamically stable systems among phototrophic microorganisms, capable of withstanding temperatures up to 70 °C and pressures exceeding 11 kbar.

01 Nov 2024·Plant Physiology and Biochemistry

Monitoring molecular events during photo-driven ubiquinone pool reduction in PufX+ and PufX− membranes from Rhobobacter capsulatus by time-resolved FTIR difference spectroscopy

Article

Author: Beatty, J. Thomas ; Johnson, Jeanette A. ; Johnson, Jeanette A ; Mezzetti, Alberto ; Beatty, J Thomas ; Leibl, Winfried

The PufX protein is found in the photosynthetic membranes of several purple bacteria and is involved in ubiquinol-ubiquinone exchange at the Q_B site of the reaction center. We have studied quinone pool reduction in chromatophores from PufX⁺ and PufX^- strains of Rhodobacter capsulatus by time-resolved FTIR difference spectroscopy under and after continuous illumination. To our knowledge, it is the first time that quinone pool reduction has been directly followed in real time in Rba. capsulatus membranes. Thanks to the availability in the literature of IR marker bands for protein conformational changes, ubiquinone consumption, ubiquinol production, Q---QH₂ quinhydrone complex formation, as well as for RC-bound Q_A^- and Q_B^- semiquinone species, it is possible to follow all the molecular events associated with light-induced quinone pool reduction. In Rba. capsulatus PufX ⁺ chromatophores, these events resemble the ones found in Rba. sphaeroides wild-type membranes. In PufX^- chromatophores the situation is different. Spectra recorded during 22.7 s of illumination showed a much smaller amount of photoreduced quinol, consistent with previous observations that PufX is required for efficient QH₂^/Q exchange at the Q_B site of the RC. Q consumption and QH₂ formation are rapidly associated with Q_A^- formation, showing that the structure of the RC-LH1 complex in PufX^- membranes does not provide efficient access to the Q_B site of the RC to a large fraction of the quinone pool, evidently because the LH1 ring increases in size to impair access to the RC. The presence of a positive band at 1560 cm^-1 suggests also the transient formation, in a fraction of chromatophores or of RC-LH1 complexes, of a Q---QH₂ quinhydrone complex. Experiments carried out after 2-flash and 10-flash sequences make it possible to estimate that the size of the quinone pool with access to the Q_B site in PufX^- membranes is ≥ 5 ubiquinone molecules per RC. The results are discussed in the framework of the current knowledge of protein organization and quinone pool reduction in bacterial photosynthetic membranes.

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PLOD1

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