2ayi
From Proteopedia
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|PDB= 2ayi |SIZE=350|CAPTION= <scene name='initialview01'>2ayi</scene>, resolution 3.70Å | |PDB= 2ayi |SIZE=350|CAPTION= <scene name='initialview01'>2ayi</scene>, resolution 3.70Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= AmpT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | |GENE= AmpT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1zjc|1ZJC]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ayi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayi OCA], [http://www.ebi.ac.uk/pdbsum/2ayi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ayi RCSB]</span> | ||
}} | }} | ||
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[[Category: Rybin, V.]] | [[Category: Rybin, V.]] | ||
[[Category: Sabala, I.]] | [[Category: Sabala, I.]] | ||
- | [[Category: ZN]] | ||
[[Category: aminopeptidase]] | [[Category: aminopeptidase]] | ||
[[Category: metallopeptidase]] | [[Category: metallopeptidase]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:59:02 2008'' |
Revision as of 22:59, 30 March 2008
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, resolution 3.70Å | |||||||
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Ligands: | |||||||
Gene: | AmpT (Thermus thermophilus) | ||||||
Related: | 1ZJC
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Wild-type AmpT from Thermus thermophilus
Overview
Aminopeptidase T (AmpT) from Thermus thermophilus is a metalloexopeptidase with no similarity to prototypical metallopeptidases with an HExxH or HxxEH motif. The crystal structure of the Staphylococcus aureus homologue of AmpT, which is known as aminopeptidase S (AmpS), has been reported recently. This structure revealed a dimeric protein with a very unusual, elongated shape and a large internal cavity. The active sites were found on the inner walls of the cavity and were entirely shielded from the environment, which suggested either that the dimer in the crystals was not physiologically relevant, or that an inactive conformation had been crystallized. Here, we show by gel-filtration and analytical ultracentrifugation that AmpT, like AmpS, forms dimers in solution, and we present the structure of AmpT in a crystal form with five protomers in the asymmetric unit. The five protomers take conformations that range from fully closed, as in the AmpS structure, to nearly open, so that the active site is almost directly accessible. The different conformations indicate flexibility between the AmpT N and C-domains, and explain how AmpT can be active, although the unusual AmpS dimerization mode applies to AmpT as well.
About this Structure
2AYI is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Substrate access to the active sites in aminopeptidase T, a representative of a new metallopeptidase clan., Odintsov SG, Sabala I, Bourenkov G, Rybin V, Bochtler M, J Mol Biol. 2005 Nov 25;354(2):403-12. Epub 2005 Sep 30. PMID:16242715
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