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6ov8

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<StructureSection load='6ov8' size='340' side='right'caption='[[6ov8]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
<StructureSection load='6ov8' size='340' side='right'caption='[[6ov8]], [[Resolution|resolution]] 2.61&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6ov8]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OV8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OV8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6ov8]] is a 6 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=6OV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OV8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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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]] 2.61&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6oad|6oad]]</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=6ov8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ov8 OCA], [https://pdbe.org/6ov8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ov8 RCSB], [https://www.ebi.ac.uk/pdbsum/6ov8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ov8 ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pepB, yfhI, b2523, JW2507 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/PepB_aminopeptidase PepB aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.23 3.4.11.23] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ov8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ov8 OCA], [http://pdbe.org/6ov8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ov8 RCSB], [http://www.ebi.ac.uk/pdbsum/6ov8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ov8 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PEPB_ECOLI PEPB_ECOLI]] Probably plays an important role in intracellular peptide degradation (PubMed:20067529).[HAMAP-Rule:MF_00504]<ref>PMID:20067529</ref>
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[https://www.uniprot.org/uniprot/PEPB_ECOLI PEPB_ECOLI] Probably plays an important role in intracellular peptide degradation (PubMed:20067529).[HAMAP-Rule:MF_00504]<ref>PMID:20067529</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Protein degradation by aminopeptidases is involved in bacterial responses to stress. Escherichia coli produces two metal-dependent M17 family leucine aminopeptidases (LAPs), aminopeptidase A (PepA) and aminopeptidase B (PepB). Several structures have been solved for PepA as well as other bacterial M17 peptidases. Herein, we report the first structures of a PepB M17 peptidase. The E. coli PepB protein structure was determined at a resolution of 2.05 and 2.6 A. One structure has both Zn(2+) and Mn(2+) , while the second structure has two Zn(2+) ions bound to the active site. A 2.75 A apo structure is also reported for PepB from Yersinia pestis. Both proteins form homohexamers, similar to the overall arrangement of PepA and other M17 peptidases. However, the divergent N-terminal domain in PepB is much larger resulting in a tertiary structure that is more expanded. Modeling of a dipeptide substrate into the C-terminal LAP domain reveals contacts that account for PepB to uniquely cleave after aspartate.
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Comparison of metal-bound and unbound structures of aminopeptidase B proteins from Escherichia coli and Yersinia pestis.,Minasov G, Lam MR, Rosas-Lemus M, Slawek J, Woinska M, Shabalin IG, Shuvalova L, Palsson BO, Godzik A, Minor W, Satchell KJF Protein Sci. 2020 Jul;29(7):1618-1628. doi: 10.1002/pro.3876. Epub 2020 May 8. PMID:32306515<ref>PMID:32306515</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6ov8" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: PepB aminopeptidase]]
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[[Category: Grimshaw S]]
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[[Category: Structural genomic]]
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[[Category: Kiryukhina O]]
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[[Category: Grimshaw, S]]
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[[Category: Kwon K]]
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[[Category: Kiryukhina, O]]
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[[Category: Minasov G]]
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[[Category: Kwon, K]]
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[[Category: Satchell KJF]]
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[[Category: Minasov, G]]
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[[Category: Shuvalova L]]
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[[Category: Satchell, K J.F]]
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[[Category: Wawrzak Z]]
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[[Category: Shuvalova, L]]
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[[Category: Wawrzak, Z]]
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[[Category: Aminopeptidase b]]
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[[Category: Csgid]]
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[[Category: Hydrolase]]
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Current revision

2.6 Angstrom Resolution Crystal Structure of Aminopeptidase B from Escherichia coli str. K-12 substr. MG1655

PDB ID 6ov8

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