1ZNO
Crystal Structure of VC702 from Vibrio Cholerae, Northeast Structural Genomics Consortium Target: VcP1
Summary for 1ZNO
| Entry DOI | 10.2210/pdb1zno/pdb |
| Descriptor | Hypothetical UPF0244 protein VC0702, MAGNESIUM ION (3 entities in total) |
| Functional Keywords | mixed alpha/beta sandwich, homodimer, structural genomics, psi, protein structure initiative, northeast structural genomics consortium, nesg, unknown function |
| Biological source | Vibrio cholerae |
| Total number of polymer chains | 2 |
| Total formula weight | 41812.86 |
| Authors | Ni, S.,Forouhar, F.,Bussiere, D.E.,Robinson, H.,Kennedy, M.A.,Northeast Structural Genomics Consortium (NESG) (deposition date: 2005-05-11, release date: 2006-07-04, Last modification date: 2024-11-13) |
| Primary citation | Ni, S.,Forouhar, F.,Bussiere, D.E.,Robinson, H.,Kennedy, M.A. Crystal structure of VC0702 at 2.0 A: conserved hypothetical protein from Vibrio cholerae. Proteins, 63:733-741, 2006 Cited by PubMed Abstract: VC0702, a conserved hypothetical protein of unknown function from Vibrio cholerae, resides in a three-gene operon containing the MbaA gene that encodes for a GGDEF and EAL domain-containing protein which is involved in regulating formation of the extracellular matrix of biofilms in Vibrio cholerae. The VC0702 crystal structure has been determined at 2.0 A and refined to Rwork = 22.8% and Rfree = 26.3%. VC0702 crystallized in an orthorhombic crystal lattice in the C222(1) space group with dimensions of a = 66.61 A, b = 88.118 A, and c = 118.35 A with a homodimer in the asymmetric unit. VC0702, which forms a mixed alpha + beta three-layered alphabetaalpha sandwich, belongs to the Pfam DUF84 and COG1986 families of proteins. Sequence conservation within the DUF84 and COG1986 families was used to identify a conserved patch of surface residues that define a cleft and potential substrate-binding site in VC0702. The three-dimensional structure of VC0702 is similar to that of Mj0226 from Methanococcus janeschii, which has been identified as a novel NTPase that binds NTP in a deep cleft similarly located to the conserved patch of surface residues that define an analogous cleft in VC0702. Collectively, the data suggest that VC0702 may have a biochemical function that involves NTP binding and phosphatase activity of some kind, and is likely involved in regulation of the signaling pathway that controls biofilm formation and maintenance in Vibrio cholerae. PubMed: 16498616DOI: 10.1002/prot.20919 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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