2ayi: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(10 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:2ayi.gif|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_2ayi", creates the "Structure Box" on the page.
You may change the PDB parameter (which sets the PDB file loaded into the applet)
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
or leave the SCENE parameter empty for the default display.
-->
{{STRUCTURE_2ayi|  PDB=2ayi  |  SCENE=  }}
'''Wild-type AmpT from Thermus thermophilus'''


==Wild-type AmpT from Thermus thermophilus==
<StructureSection load='2ayi' size='340' side='right'caption='[[2ayi]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ayi]] is a 5 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AYI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ayi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ayi OCA], [https://pdbe.org/2ayi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ayi RCSB], [https://www.ebi.ac.uk/pdbsum/2ayi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ayi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMPT_THET8 AMPT_THET8] Metal-dependent exopeptidase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ay/2ayi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2ayi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:16242715</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 2ayi" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Bochtler, M.]]
[[Category: Bochtler M]]
[[Category: Bourenkov, G.]]
[[Category: Bourenkov G]]
[[Category: Odintsov, S G.]]
[[Category: Odintsov SG]]
[[Category: Rybin, V.]]
[[Category: Rybin V]]
[[Category: Sabala, I.]]
[[Category: Sabala I]]
[[Category: Aminopeptidase]]
[[Category: Metallopeptidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 19:37:41 2008''