2ayi

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[[Image:2ayi.gif|left|200px]]<br /><applet load="2ayi" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ayi.gif|left|200px]]
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caption="2ayi, resolution 3.70&Aring;" />
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'''Wild-type AmpT from Thermus thermophilus'''<br />
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{{Structure
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|PDB= 2ayi |SIZE=350|CAPTION= <scene name='initialview01'>2ayi</scene>, resolution 3.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY=
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|GENE= AmpT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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}}
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'''Wild-type AmpT from Thermus thermophilus'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AYI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYI OCA].
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2AYI is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AYI OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16242715 16242715]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16242715 16242715]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
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[[Category: metallopeptidase]]
[[Category: metallopeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:20 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:55:25 2008''

Revision as of 13:55, 20 March 2008


PDB ID 2ayi

Drag the structure with the mouse to rotate
, resolution 3.70Å
Ligands:
Gene: AmpT (Thermus thermophilus)
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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