3T5C

Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2

3T5C の概要

• エントリーDOI: 10.2210/pdb3t5c/pdb
• 関連するPDBエントリー: 3T5A 3T5B
• 分子名称: PROBABLE CHAIN-FATTY-ACID-CoA LIGASE FADD13 (2 entities in total)
• 機能のキーワード: acetyl-coa synthetase like fold, ligase, amp-binding
• 由来する生物種: Mycobacterium tuberculosis
• 細胞内の位置: Cell membrane; Peripheral membrane protein: O53306
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85683.55

構造登録者

Goyal, A.,Sankaranarayanan, R. (登録日: 2011-07-27, 公開日: 2012-01-25, 最終更新日: 2023-11-01)

主引用文献

Goyal, A.,Verma, P.,Anandhakrishnan, M.,Gokhale, R.S.,Sankaranarayanan, R.
Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis.
J.Mol.Biol., 416:221-238, 2012

PubMed Abstract: Activation of fatty acids as acyl-adenylates by fatty acyl-AMP ligases (FAALs) in Mycobacterium tuberculosis is a variant of a classical theme that involves formation of acyl-CoA (coenzyme A) by fatty acyl-CoA ligases (FACLs). Here, we show that FAALs and FACLs possess similar structural fold and substrate specificity determinants, and the key difference is the absence of a unique insertion sequence in FACL13 structure. A systematic analysis shows a conserved hydrophobic anchorage of the insertion motif across several FAALs. Strikingly, mutagenesis of two phenylalanine residues, which are part of the anchorage, to alanine converts FAAL32 to FACL32. This insertion-based in silico analysis suggests the presence of FAAL homologues in several other non-mycobacterial genomes including eukaryotes. The work presented here establishes an elegant mechanism wherein an insertion sequence drives the functional divergence of FAALs from canonical FACLs.

PubMed: 22206988
DOI: 10.1016/j.jmb.2011.12.031

実験手法

X-RAY DIFFRACTION (2.09 Å)