2GX8

The Crystal Structure of Bacillus cereus protein related to NIF3

Summary for 2GX8

• Entry DOI: 10.2210/pdb2gx8/pdb
• Descriptor: NIF3-related protein, ZINC ION, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, ... (5 entities in total)
• Functional Keywords: structural genomics, unknown function, nif3 related protein, psi, protein structure initiative, midwest center for structural genomics, mcsg
• Biological source: Bacillus cereus
• Total number of polymer chains: 3
• Total formula weight: 132658.49

Authors

Minasov, G.,Brunzelle, J.S.,Shuvalova, L.,Vorontsov, I.I.,Collart, F.R.,Joachimiak, A.,Anderson, W.F.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2006-05-08, release date: 2006-05-16, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.2 Å)