2oxr
From Proteopedia
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- | [[Image:2oxr.gif|left|200px]] | + | [[Image:2oxr.gif|left|200px]] |
- | + | ||
- | '''PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi (after GTP hydrolysis)''' | + | {{Structure |
+ | |PDB= 2oxr |SIZE=350|CAPTION= <scene name='initialview01'>2oxr</scene>, resolution 2.40Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= pab0955 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29292 Pyrococcus abyssi]) | ||
+ | }} | ||
+ | |||
+ | '''PAB0955 crystal structure : a GTPase in GDP and Mg bound form from Pyrococcus abyssi (after GTP hydrolysis)''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2OXR is a [ | + | 2OXR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OXR OCA]. |
==Reference== | ==Reference== | ||
- | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17468740 17468740] |
[[Category: Pyrococcus abyssi]] | [[Category: Pyrococcus abyssi]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rossman fold]] | [[Category: rossman fold]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:06:00 2008'' |
Revision as of 16:06, 20 March 2008
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, resolution 2.40Å | |||||||
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Ligands: | and | ||||||
Gene: | pab0955 (Pyrococcus abyssi) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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.
About this Structure
2OXR is a Single protein structure of sequence from Pyrococcus abyssi. Full crystallographic information is available from OCA.
Reference
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 Thu Mar 20 18:06:00 2008
Categories: Pyrococcus abyssi | Single protein | Armengaud, J. | Carpentier, P. | Gras, S. | Housset, D. | GDP | MG | Gdp | Gtp binding protein | Gtpase | Hydrolase | P-loop | Rossman fold