2bn7: Difference between revisions

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-[[Image:2bn7.jpg|left|200px]]<br /><applet load="2bn7" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2bn7, resolution 2.40&Aring;" />
-'''MN SUBSTITUTED E. COLI AMINOPEPTIDASE P IN COMPLEX WITH PRODUCT AND ZN'''<br />
-==Overview==
+==Mn substituted E. coli Aminopeptidase P in complex with product and Zn==
-The effect of metal substitution on the activity and structure of the, aminopeptidase P (APPro) from Escherichia coli has been investigated., Measurements of activity in the presence of Mn2+, Mg2+, Zn2+, Na+, and, Ca2+ show that significant activity is seen only in the Mn-bound form of, the enzyme. The addition of Zn2+ to [MnMn(APPro)] is strongly inhibitory., Crystal structures of [MnMn(APPro)], [MgMg(APPro)], [ZnZn(APPro)], [ZnMg(APPro)], [Ca_(APPro)], [Na_(APPro)], and [apo(APPro)] were, determined. The structures of [Ca_(APPro)] and [Na_(APPro)] have a single, metal atom at their active site. Surprisingly, when a tripeptide substrate, (ValProLeu) was soaked into [Na_(APPro)] crystals in the presence of 200, mM Mg2+, the structure had substrate, but no metal, bound at the active, site. The structure of apo APPro complexed with ValProLeu shows that the, N-terminal amino group of a substrate can be bound at the active site by, carboxylate side chains that normally bind the second metal atom, providing a model for substrate binding in a single-metal active enzyme., Structures of [MnMn(APPro)] and [ZnZn(APPro)] complexes of ProLeu, a, product inhibitor, in the presence of excess Zn reveal a third, metal-binding site, formed by two conserved His residues and the dipeptide, inhibitor. A Zn atom bound at such a site would stabilize product binding, and enhance inhibition.
+<StructureSection load='2bn7' size='340' side='right'caption='[[2bn7]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2bn7]] 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=2BN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BN7 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=LEU:LEUCINE'>LEU</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bn7 OCA], [https://pdbe.org/2bn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bn7 RCSB], [https://www.ebi.ac.uk/pdbsum/2bn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bn7 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/AMPP_ECOLI AMPP_ECOLI]
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bn/2bn7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=2bn7 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The effect of metal substitution on the activity and structure of the aminopeptidase P (APPro) from Escherichia coli has been investigated. Measurements of activity in the presence of Mn2+, Mg2+, Zn2+, Na+, and Ca2+ show that significant activity is seen only in the Mn-bound form of the enzyme. The addition of Zn2+ to [MnMn(APPro)] is strongly inhibitory. Crystal structures of [MnMn(APPro)], [MgMg(APPro)], [ZnZn(APPro)], [ZnMg(APPro)], [Ca_(APPro)], [Na_(APPro)], and [apo(APPro)] were determined. The structures of [Ca_(APPro)] and [Na_(APPro)] have a single metal atom at their active site. Surprisingly, when a tripeptide substrate (ValProLeu) was soaked into [Na_(APPro)] crystals in the presence of 200 mM Mg2+, the structure had substrate, but no metal, bound at the active site. The structure of apo APPro complexed with ValProLeu shows that the N-terminal amino group of a substrate can be bound at the active site by carboxylate side chains that normally bind the second metal atom, providing a model for substrate binding in a single-metal active enzyme. Structures of [MnMn(APPro)] and [ZnZn(APPro)] complexes of ProLeu, a product inhibitor, in the presence of excess Zn reveal a third metal-binding site, formed by two conserved His residues and the dipeptide inhibitor. A Zn atom bound at such a site would stabilize product binding and enhance inhibition.
-==About this Structure==
+Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center.,Graham SC, Bond CS, Freeman HC, Guss JM Biochemistry. 2005 Oct 25;44(42):13820-36. PMID:16229471<ref>PMID:16229471</ref>
-BN7 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 MN, FLC, ZN, MG and PRO as [http://en.wikipedia.org/wiki/ligands ligands]. 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=AC1:LEU Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BN7 OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-Structural and functional implications of metal ion selection in aminopeptidase P, a metalloprotease with a dinuclear metal center., Graham SC, Bond CS, Freeman HC, Guss JM, Biochemistry. 2005 Oct 25;44(42):13820-36. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16229471 16229471]
+</div>
+<div class="pdbe-citations 2bn7" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Escherichia coli]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Xaa-Pro aminopeptidase]]
+[[Category: Bond CS]]
-[[Category: Bond, C.S.]]
+[[Category: Freeman HC]]
-[[Category: Freeman, H.C.]]
+[[Category: Graham SC]]
-[[Category: Graham, S.C.]]
+[[Category: Guss JM]]
-[[Category: Guss, J.M.]]
-[[Category: FLC]]
-[[Category: MG]]
-[[Category: MN]]
-[[Category: PRO]]
-[[Category: ZN]]
-[[Category: dinuclear hydrolase]]
-[[Category: metalloenzyme]]
-[[Category: pita-bread fold]]
-[[Category: product complex]]
-[[Category: proline-specific peptidase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:53:05 2007''