1a16

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[[Image:1a16.gif|left|200px]]<br /><applet load="1a16" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1a16, resolution 2.3&Aring;" />
 
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'''AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU'''<br />
 
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==Overview==
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==AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU==
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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, Xaa-Pro. The metal-binding residues are located in a single subunit, but, the residues surrounding the active site are contributed by three, subunits. The fold of the protein resembles that of creatine, amidinohydrolase (creatinase, not a metalloenzyme). The C-terminal, catalytic domain is also similar to the single-domain enzyme methionine, aminopeptidase that has a dinuclear cobalt center.
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<StructureSection load='1a16' size='340' side='right'caption='[[1a16]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1a16]] 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=1A16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A16 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a16 OCA], [https://pdbe.org/1a16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a16 RCSB], [https://www.ebi.ac.uk/pdbsum/1a16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a16 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMPP_ECOLI AMPP_ECOLI]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a1/1a16_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1a16 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1A16 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 <scene name='pdbligand=MN:'>MN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Xaa-Pro_aminopeptidase Xaa-Pro aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.9 3.4.11.9] Known structural/functional Site: <scene name='pdbsite=NUL:These+Residues+Coordinate+The+Mn+Ions'>NUL</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A16 OCA].
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Xaa-Pro aminopeptidase]]
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[[Category: Bond CS]]
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[[Category: Bond, C.S.]]
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[[Category: Dixon NE]]
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[[Category: Dixon, N.E.]]
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[[Category: Freeman HC]]
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[[Category: Freeman, H.C.]]
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[[Category: Guss JM]]
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[[Category: Guss, J.M.]]
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[[Category: Lilley PE]]
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[[Category: Lilley, P.E.]]
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[[Category: Wilce MC]]
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[[Category: Wilce, M.C.]]
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[[Category: MN]]
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[[Category: complex (proline peptidase/inhibitor)]]
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[[Category: proline peptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:28:37 2008''
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Current revision

AMINOPEPTIDASE P FROM E. COLI WITH THE INHIBITOR PRO-LEU

PDB ID 1a16

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