1m35: Difference between revisions
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==Aminopeptidase P from Escherichia coli== | ==Aminopeptidase P from Escherichia coli== | ||
<StructureSection load='1m35' size='340' side='right' caption='[[1m35]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1m35' size='340' side='right'caption='[[1m35]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1m35]] is a 6 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1m35]] is a 6 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=1M35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M35 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1m35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m35 OCA], [https://pdbe.org/1m35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m35 RCSB], [https://www.ebi.ac.uk/pdbsum/1m35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m35 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/AMPP_ECOLI AMPP_ECOLI] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m3/1m35_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/m3/1m35_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1m35 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 30: | Line 31: | ||
==See Also== | ==See Also== | ||
*[[Aminopeptidase|Aminopeptidase]] | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Freeman | [[Category: Freeman HC]] | ||
[[Category: Graham | [[Category: Graham SC]] | ||
[[Category: Guss | [[Category: Guss JM]] | ||
[[Category: Lee | [[Category: Lee M]] | ||
Latest revision as of 12:16, 16 August 2023
Aminopeptidase P from Escherichia coliAminopeptidase P from Escherichia coli
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedAminopeptidase P (AMPP) from Escherichia coli cleaves the N-terminal residue from an oligopeptide if the second residue is proline. The active site contains a dinuclear metal centre. Following earlier structural analyses of crystals in space groups P6(4)22 and I4(1)22, the structure of AMPP has been solved and refined in the orthorhombic space group C222(1) at 2.4 A resolution. There are six subunits in the asymmetric unit. These are arranged in two types of tetramer. One tetramer comprises four crystallographically independent subunits, while the other comprises two pairs of subunits related by a crystallographic twofold axis. The final model of 20 994 protein atoms, 1618 water molecules and 12 metal atoms refined to residuals R = 0.195 and R(free) = 0.215. The molecular structure confirms most of the previously reported features, including the subunit-subunit interfaces in the tetramer and persistent disorder at some residues. The metal-ligand bond lengths at the active site suggest that one of the two Mn atoms is five-coordinate rather than six-coordinate. An orthorhombic form of Escherichia coli aminopeptidase P at 2.4 A resolution.,Graham SC, Lee M, Freeman HC, Guss JM Acta Crystallogr D Biol Crystallogr. 2003 May;59(Pt 5):897-902. Epub 2003, Apr 25. PMID:12777807[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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