This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2hjg
From Proteopedia
Revision as of 02:21, 29 September 2014 by OCA (Talk | contribs)
2hjg is a 1 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of a Bacillus subtilis YphC/GDP complex shows that it contains two GTPase domains that pack against a central domain whose fold resembles that of an RNA binding KH-domain. Comparisons of this structure to that of a homologue in Thermotoga maritima reveals a dramatic rearrangement in the position of the N-terminal GTPase domain with a shift of up to 60 A and the formation of a totally different interface to the central domain. This rearrangement appears to be triggered by conformational changes of the switch II region in this domain in response to nucleotide binding. Modeling studies suggest that this motion represents transitions between the "on" and "off" states of the GTPase, the effect of which is to alternately expose and bury a positively charged face of the central domain that we suggest is involved in RNA recognition as part of the possible role of this enzyme in ribosome binding.
The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding.,Muench SP, Xu L, Sedelnikova SE, Rice DW Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12359-64. Epub 2006 Aug 7. PMID:16894162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Muench SP, Xu L, Sedelnikova SE, Rice DW. The essential GTPase YphC displays a major domain rearrangement associated with nucleotide binding. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12359-64. Epub 2006 Aug 7. PMID:16894162
