Description
Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.2
Classification:STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Release Date:2006-05-16
Deposition Date:2006-05-08
Revision Date:2008-05-01#2011-07-13#2017-02-01#2017-10-18
Molecular Weight:132658.48
Macromolecule Type:Protein
Residue Count:1191
Atom Site Count:8467
DOI:10.2210/pdb2gx8/pdb
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.
Resolution:2.2
Classification:STRUCTURAL GENOMICS, UNKNOWN FUNCTION
Release Date:2006-05-16
Deposition Date:2006-05-08
Revision Date:2008-05-01#2011-07-13#2017-02-01#2017-10-18
Molecular Weight:132658.48
Macromolecule Type:Protein
Residue Count:1191
Atom Site Count:8467
DOI:10.2210/pdb2gx8/pdb
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.
| Date made available | 2006 |
|---|---|
| Publisher | RCSB-PDB |