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6LIX

CRL Protein of Arabidopsis

6LIX の概要
エントリーDOI10.2210/pdb6lix/pdb
分子名称Chromophore lyase CRL, chloroplastic, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total)
機能のキーワードa homolog of cyanobacterial cpct lyase, plant protein, lyase
由来する生物種Arabidopsis thaliana (Mouse-ear cress)
タンパク質・核酸の鎖数2
化学式量合計61128.76
構造登録者
Wang, F.F.,Guan, K.L.,Sun, P.K.,Xing, W.M. (登録日: 2019-12-13, 公開日: 2020-09-16, 最終更新日: 2024-10-30)
主引用文献Wang, F.,Fang, J.,Guan, K.,Luo, S.,Dogra, V.,Li, B.,Ma, D.,Zhao, X.,Lee, K.P.,Sun, P.,Xin, J.,Liu, T.,Xing, W.,Kim, C.
The Arabidopsis CRUMPLED LEAF protein, a homolog of the cyanobacterial bilin lyase, retains the bilin-binding pocket for a yet unknown function.
Plant J., 104:964-978, 2020
Cited by
PubMed Abstract: The photosynthetic bacterial phycobiliprotein lyases, also called CpcT lyases, catalyze the biogenesis of phycobilisome, a light-harvesting antenna complex, through the covalent attachment of chromophores to the antenna proteins. The Arabidopsis CRUMPLED LEAF (CRL) protein is a homolog of the cyanobacterial CpcT lyase. Loss of CRL leads to multiple lesions, including localized foliar cell death, constitutive expression of stress-related nuclear genes, abnormal cell cycle, and impaired plastid division. Notwithstanding the apparent phenotypes, the function of CRL still remains elusive. To gain insight into the function of CRL, we examined whether CRL still retains the capacity to bind with the bacterial chromophore phycocyanobilin (PCB) and its plant analog phytochromobilin (PΦB). The revealed structure of the CpcT domain of CRL is comparable to that of the CpcT lyase, despite the low sequence identity. The subsequent in vitro biochemical assays found, as shown for the CpcT lyase, that PCB/PΦB binds to the CRL dimer. However, some mutant forms of CRL, substantially compromised in their bilin-binding ability, still restore the crl-induced multiple lesions. These results suggest that although CRL retains the bilin-binding pocket, it seems not functionally associated with the crl-induced multiple lesions.
PubMed: 32860438
DOI: 10.1111/tpj.14974
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.385 Å)
構造検証レポート
Validation report summary of 6lix
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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