2oxr: Difference between revisions

Revision as of 14:01, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2oxr.png

Template:STRUCTURE 2oxr

PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi (after GTP hydrolysis)PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi (after GTP hydrolysis)

Template:ABSTRACT PUBMED 17468740

About this StructureAbout this Structure

2OXR is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.

ReferenceReference

Structural insights into a new homodimeric self-activated GTPase family., Gras S, Chaumont V, Fernandez B, Carpentier P, Charrier-Savournin F, Schmitt S, Pineau C, Flament D, Hecker A, Forterre P, Armengaud J, Housset D, EMBO Rep. 2007 Jun;8(6):569-75. Epub 2007 Apr 20. PMID:17468740

Page seeded by OCA on Sun Jul 27 14:01:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2oxr.gif|left|200px]]
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 {{STRUCTURE_2oxr|  PDB=2oxr  |  SCENE=  }}
-'''PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi (after GTP hydrolysis)'''
+===PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi (after GTP hydrolysis)===
-==Overview==
+<!--
-The human XAB1/MBDin GTPase and its close homologues form one of the ten phylogenetically distinct families of the SIMIBI (after signal recognition particle, MinD and BioD) class of phosphate-binding loop NTPases. The genomic context and the partners identified for the archaeal and eukaryotic homologues indicate that they are involved in genome maintenance--DNA repair or replication. The crystal structure of PAB0955 from Pyrococcus abyssi shows that, unlike other SIMIBI class G proteins, these highly conserved GTPases are homodimeric, regardless of the presence of nucleotides. The nucleotide-binding site of PAB0955 is rather rigid and its conformation is closest to that of the activated SRP G domain. One insertion to the G domain bears a strictly conserved GPN motif, which is part of the catalytic site of the other monomer and stabilizes the phosphate ion formed. Owing to this unique functional feature, we propose to call this family as GPN-loop GTPase.
+The line below this paragraph, {{ABSTRACT_PUBMED_17468740}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17468740 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17468740}}
 ==About this Structure==
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 [[Category: P-loop]]
 [[Category: Rossman fold]]
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