2GX8

The Crystal Structure of Bacillus cereus protein related to NIF3

2GX8 の概要

• エントリーDOI: 10.2210/pdb2gx8/pdb
• 分子名称: NIF3-related protein, ZINC ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total)
• 機能のキーワード: structural genomics, unknown function, nif3 related protein, psi, protein structure initiative, midwest center for structural genomics, mcsg
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 132658.49

構造登録者

Minasov, G.,Brunzelle, J.S.,Shuvalova, L.,Vorontsov, I.I.,Collart, F.R.,Joachimiak, A.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (登録日: 2006-05-08, 公開日: 2006-05-16, 最終更新日: 2024-02-14)

主引用文献

Godsey, M.H.,Minasov, G.,Shuvalova, L.,Brunzelle, J.S.,Vorontsov, I.I.,Collart, F.R.,Anderson, W.F.
The 2.2 A resolution crystal structure of Bacillus cereus Nif3-family protein YqfO reveals a conserved dimetal-binding motif and a regulatory domain
Protein Sci., 16:1285-1293, 2007

PubMed Abstract: YqfO of Bacillus cereus is a member of the widespread Nif3 family of proteins, which has been highlighted as an important target for structural genomics. The N- and C-terminal domains are conserved across the family and contain a dimetal-binding motif in a putative active site. YqfO contains an insert in the middle of the protein, present in a minority of bacterial family members. The structure of YqfO was determined at a resolution of 2.2 A and reveals conservation of the putative active site. It also reveals the previously unknown structure of the insert, which despite extremely limited sequence conservation, bears great similarity to PII, CutA, and a number of other trimeric regulatory proteins. Our results suggest that this domain acts as a signal sensor to regulate the still-unknown catalytic activity of the more-conserved domains.

PubMed: 17586767
DOI: 10.1110/ps.062674007

実験手法

X-RAY DIFFRACTION (2.2 Å)