1jaw: Difference between revisions

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[[Image:1jaw.gif|left|200px]]<br />
<applet load="1jaw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1jaw, resolution 2.7&Aring;" />
'''AMINOPEPTIDASE P FROM E. COLI LOW PH FORM'''<br />


==Overview==
==AMINOPEPTIDASE P FROM E. COLI LOW PH FORM==
The structure of the proline-specific aminopeptidase (EC 3.4.11.9) from, Escherichia coli has been solved and refined for crystals of the native, enzyme at a 2.0-A resolution, for a dipeptide-inhibited complex at 2.3-A, resolution, and for a low-pH inactive form at 2.7-A resolution. The, protein crystallizes as a tetramer, more correctly a dimer of dimers, at, both high and low pH, consistent with observations from analytical, ultracentrifuge studies that show that the protein is a tetramer under, physiological conditions. The monomer folds into two domains. The active, site, in the larger C-terminal domain, contains a dinuclear manganese, center in which a bridging water molecule or hydroxide ion appears poised, to act as the nucleophile in the attack on the scissile peptide bond of, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9520390 (full description)]]
<StructureSection load='1jaw' size='340' side='right'caption='[[1jaw]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jaw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JAW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JAW 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]] 2.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</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=1jaw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jaw OCA], [https://pdbe.org/1jaw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jaw RCSB], [https://www.ebi.ac.uk/pdbsum/1jaw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jaw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMPP_ECOLI AMPP_ECOLI]
== 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/ja/1jaw_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=1jaw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1JAW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]] with MN and ACT as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Hydrolase Hydrolase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JAW OCA]].
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Structure and mechanism of a proline-specific aminopeptidase from Escherichia coli., Wilce MC, Bond CS, Dixon NE, Freeman HC, Guss JM, Lilley PE, Wilce JA, Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3472-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9520390 9520390]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bond, C.S.]]
[[Category: Bond CS]]
[[Category: Dixon, N.E.]]
[[Category: Dixon NE]]
[[Category: Freeman, H.C.]]
[[Category: Freeman HC]]
[[Category: Guss, J.M.]]
[[Category: Guss JM]]
[[Category: Lilley, P.E.]]
[[Category: Lilley PE]]
[[Category: Wilce, M.C.J.]]
[[Category: Wilce MCJ]]
[[Category: ACT]]
[[Category: MN]]
[[Category: aminopeptidase]]
[[Category: hydrolase]]
[[Category: proline peptidase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 08:27:59 2007''

Latest revision as of 07:38, 7 February 2024

AMINOPEPTIDASE P FROM E. COLI LOW PH FORM

1jaw, resolution 2.70Å

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