2hpo

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[[Image:2hpo.gif|left|200px]]
 
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{{Structure
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==Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site==
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|PDB= 2hpo |SIZE=350|CAPTION= <scene name='initialview01'>2hpo</scene>, resolution 1.65&Aring;
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<StructureSection load='2hpo' size='340' side='right'caption='[[2hpo]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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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|GENE= pepN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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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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|DOMAIN=
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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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|RELATEDENTRY=
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hpo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hpo OCA], [http://www.ebi.ac.uk/pdbsum/2hpo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hpo RCSB]</span>
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== Function ==
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}}
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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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'''Structure of Aminopeptidase N from E. coli Suggests a Compartmentalized, Gated Active Site'''
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==See Also==
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Escherichia coli K-12]]
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[[Category: Large Structures]]
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==About this Structure==
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[[Category: Addlagatta A]]
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2HPO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HPO OCA].
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[[Category: Gay L]]
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[[Category: Matthews BW]]
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/16938892 16938892]
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[[Category: Escherichia coli]]
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[[Category: Membrane alanyl aminopeptidase]]
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[[Category: Single protein]]
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[[Category: Addlagatta, A.]]
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[[Category: Gay, L.]]
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[[Category: Matthews, B W.]]
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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 Mon Mar 31 03:33:34 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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