2hpo

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[[Image:2hpo.gif|left|200px]]<br /><applet load="2hpo" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hpo, resolution 1.65&Aring;" />
 
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'''Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site'''<br />
 
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==Overview==
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==Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site==
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Aminopeptidase N from Escherichia coli is a major metalloprotease that participates in the controlled hydrolysis of peptides in the proteolytic pathway. Determination of the 870-aa structure reveals that it has four domains similar to the tricorn-interacting factor F3. The thermolysin-like active site is enclosed within a large cavity with a volume of 2,200 A(3), which is inaccessible to substrates except for a small opening of approximately 8-10 A. The substrate-based inhibitor bestatin binds to the protein with minimal changes, suggesting that this is the active form of the enzyme. The previously described structure of F3 had three distinct conformations that were described as "closed," "intermediate," and "open." The structure of aminopeptidase N from E. coli, however, is substantially more closed than any of these. Taken together, the results suggest that these proteases, which are involved in intracellular peptide degradation, prevent inadvertent hydrolysis of inappropriate substrates by enclosing the active site within a large cavity. There is also some evidence that the open form of the enzyme, which admits substrates, remains inactive until it adopts the closed form.
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<StructureSection load='2hpo' size='340' side='right'caption='[[2hpo]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hpo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HPO 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]] 1.65&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2hpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hpo OCA], [https://pdbe.org/2hpo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hpo RCSB], [https://www.ebi.ac.uk/pdbsum/2hpo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hpo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/AMPN_ECOLI AMPN_ECOLI] Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation.
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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/hp/2hpo_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=2hpo 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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2HPO 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=ZN:'>ZN</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Membrane_alanyl_aminopeptidase Membrane alanyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.2 3.4.11.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPO 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 of aminopeptidase N from Escherichia coli suggests a compartmentalized, gated active site., Addlagatta A, Gay L, Matthews BW, Proc Natl Acad Sci U S A. 2006 Sep 5;103(36):13339-44. Epub 2006 Aug 28. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16938892 16938892]
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[[Category: Escherichia coli K-12]]
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Membrane alanyl aminopeptidase]]
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[[Category: Addlagatta A]]
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[[Category: Single protein]]
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[[Category: Gay L]]
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[[Category: Addlagatta, A.]]
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[[Category: Matthews BW]]
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[[Category: Gay, L.]]
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[[Category: Matthews, B W.]]
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[[Category: GOL]]
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[[Category: ZN]]
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[[Category: closed]]
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[[Category: compartmentalized active site]]
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[[Category: multidomain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:44:24 2008''
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Current revision

Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site

PDB ID 2hpo

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