2hjb: Difference between revisions

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-[[Image:2hjb.png|left|200px]]
-{{STRUCTURE_2hjb|  PDB=2hjb  |  SCENE=  }}
+==Crystal structure of Alcaligenes faecalis AADH in complex with p-methoxybenzylamine==
+<StructureSection load='2hjb' size='340' side='right'caption='[[2hjb]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2hjb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alcfa Alcfa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HJB FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PZM:1-(4-METHOXYPHENYL)METHANAMINE'>PZM</scene></td></tr>
+<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=TRQ:2-AMINO-3-(6,7-DIOXO-6,7-DIHYDRO-1H-INDOL-3-YL)-PROPIONIC+ACID'>TRQ</scene></td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2hj4|2hj4]], [[2hj7|2hj7]], [[2hkm|2hkm]], [[2hkr|2hkr]]</div></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aralkylamine_dehydrogenase_(azurin) Aralkylamine dehydrogenase (azurin)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.9.2 1.4.9.2] </span></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=2hjb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hjb OCA], [https://pdbe.org/2hjb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hjb RCSB], [https://www.ebi.ac.uk/pdbsum/2hjb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hjb ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[https://www.uniprot.org/uniprot/AAUA_ALCFA AAUA_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:7876189</ref> <ref>PMID:17087503</ref> <ref>PMID:17005560</ref> <ref>PMID:16614214</ref>  [[https://www.uniprot.org/uniprot/AAUB_ALCFA AAUB_ALCFA]] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor.<ref>PMID:11495996</ref> <ref>PMID:16279953</ref> <ref>PMID:8188594</ref> <ref>PMID:16614214</ref>
+== 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/hj/2hjb_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=2hjb ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Structure-activity correlations have been employed previously in the mechanistic interpretation of TTQ-dependent amine dehydrogenases using a series of para-substituted benzylamines. However, by combining the use of kinetic isotope effects (KIEs) and crystallographic analysis, in conjunction with structure-reactivity correlation studies, we show that para-substituted benzylamines are poor reactivity probes for TTQ-dependent aromatic amine dehydrogenase (AADH). Stopped-flow kinetic studies of the reductive half-reaction, with para-substituted benzylamines and their dideuterated counterparts, demonstrate that C-H or C-D bond breakage is not fully rate limiting (KIEs approximately unity). Contrary to previous reports, Hammett plots exhibit a poor correlation of structure-reactivity data with electronic substituent effects for para-substituted benzylamines and phenylethylamines. Crystallographic studies of enzyme-substrate complexes reveal that the observed structure-reactivity correlations are not attributed to distinct binding modes for para-substituted benzylamines in the active site, although two binding sites for p-nitrobenzylamine are identified. We identify structural rearrangements, prior to the H-transfer step, which are likely to limit the rate of TTQ reduction by benzylamines. This work emphasizes (i) the need for caution when applying structure-activity correlations to enzyme-catalyzed reactions and (ii) the added benefit of using both isotope effects and structural analysis, in conjunction with structure-reactivity relationships, to study chemical steps in enzyme reaction cycles.
-===Crystal structure of Alcaligenes faecalis AADH in complex with p-methoxybenzylamine===
+Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase.,Hothi P, Roujeinikova A, Khadra KA, Lee M, Cullis P, Leys D, Scrutton NS Biochemistry. 2007 Aug 14;46(32):9250-9. Epub 2007 Jul 18. PMID:17636875<ref>PMID:17636875</ref>
-{{ABSTRACT_PUBMED_17636875}}
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2hjb" style="background-color:#fffaf0;"></div>
-==About this Structure==
+==See Also==
-[[2hjb]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Alcaligenes_faecalis Alcaligenes faecalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HJB OCA].
+*[[Aromatic amine dehydrogenase 3D structures|Aromatic amine dehydrogenase 3D structures]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:017636875</ref><references group="xtra"/>
+__TOC__
-[[Category: Alcaligenes faecalis]]
+</StructureSection>
-[[Category: Aralkylamine dehydrogenase]]
+[[Category: Alcfa]]
-[[Category: Leys, D.]]
+[[Category: Large Structures]]
-[[Category: Roujeinikova, A.]]
+[[Category: Leys, D]]
+[[Category: Roujeinikova, A]]
 [[Category: Oxidoreductase]]
 [[Category: P-substituted benzylamine]]