2IWR

Gtpase Like Domain Of Centaurin Gamma 1 (Human)

Summary for 2IWR

• Entry DOI: 10.2210/pdb2iwr/pdb
• Related: 2BMJ
• Descriptor: CENTAURIN GAMMA 1 (2 entities in total)
• Functional Keywords: ank repeat, zinc-finger, gtp-binding, polymorphism, nucleotide-binding, alternative splicing, protein transport, gtpase activation, hydrolase, metal-binding, nuclear protein, phosphorylation, sgc, zinc, centg1, gtpase, oncogene, transport, structual genomics consortium, structural genomics consortium, structural genomics
• Biological source: HOMO SAPIENS (HUMAN)
• Cellular location: Isoform 1: Cytoplasm. Isoform 2: Cytoplasm: Q99490
• Total number of polymer chains: 1
• Total formula weight: 19847.26

Authors

Elkins, J.M.,Soundararajan, M.,Yang, X.,Papagrigoriou, E.,Sundstrom, M.,Edwards, A.,Arrowsmith, C.,Weigelt, J.,Doyle, D.A.,Structural Genomics Consortium (SGC) (deposition date: 2006-07-03, release date: 2006-07-04, Last modification date: 2024-11-20)

Primary citation

Soundararajan, M.,Yang, X.,Elkins, J.M.,Sobott, F.,Doyle, D.A.
The Centaurin Gamma-1 Gtpase-Like Domain Functions as an Ntpase.
Biochem.J., 401:679-, 2007

PubMed Abstract: Centaurins are a family of proteins that contain GTPase-activating protein domains, with the gamma family members containing in addition a GTPase-like domain. Centaurins reside mainly in the nucleus and are known to activate phosphoinositide 3-kinase, a key regulator of cell proliferation, motility and vesicular trafficking. In the present study, using X-ray structural analysis, enzymatic assays and nucleotide-binding studies, we show that, for CENTG1 (centaurin gamma-1) the GTPase-like domain has broader trinucleotide specificity. Alterations within the G4 motif of CENTG1 from the highly conserved NKXD found in typical GTPases to TQDR result in the loss of specificity, a lower affinity for the nucleotides and higher turnover rates. These results indicate that the centaurins could be more accurately classified as NTPases and point to alternative mechanisms of cell signalling control.

PubMed: 17037982
DOI: 10.1042/BJ20060555

Experimental method

X-RAY DIFFRACTION (1.5 Å)