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3gmc

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Current revision (09:55, 21 February 2024) (edit) (undo)
 
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<StructureSection load='3gmc' size='340' side='right'caption='[[3gmc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3gmc' size='340' side='right'caption='[[3gmc]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3gmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_700743 Atcc 700743]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GMC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3gmc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesorhizobium_loti Mesorhizobium loti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GMC FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3HM:5-HYDROXY-6-METHYLPYRIDINE-3-CARBOXYLIC+ACID'>3HM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3gmb|3gmb]]</div></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=3HM:5-HYDROXY-6-METHYLPYRIDINE-3-CARBOXYLIC+ACID'>3HM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mlr6788 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=381 ATCC 700743])</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=3gmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gmc OCA], [https://pdbe.org/3gmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gmc RCSB], [https://www.ebi.ac.uk/pdbsum/3gmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gmc ProSAT]</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=3gmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gmc OCA], [https://pdbe.org/3gmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gmc RCSB], [https://www.ebi.ac.uk/pdbsum/3gmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gmc ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q988D3_RHILO Q988D3_RHILO]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=3gmc ConSurf].
</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=3gmc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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A vitamin B(6) degradative pathway has recently been identified and characterized in Mesorhizobium loti MAFF303099. One of the enzymes on this pathway, 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase (MHPCO), is a flavin-dependent enzyme and catalyzes the oxidative ring-opening of 2-methyl-3-hydroxypyridine-5-carboxylic acid to form E-2-(acetamino-methylene)succinate. The gene for this enzyme has been cloned, and the corresponding protein has been overexpressed in Escherichia coli and purified. The crystal structure of MHPCO has been solved to 2.1 A using SAD phasing with and without the substrate MHPC bound. These crystal structures provide insight into the reaction mechanism and suggest roles for active site residues in the catalysis of a novel oxidative ring-opening reaction.
 
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Structure of the PLP Degradative Enzyme 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase from Mesorhizobium loti MAFF303099 and Its Mechanistic Implications.,McCulloch KM, Mukherjee T, Begley TP, Ealick SE Biochemistry. 2009 Apr 1. PMID:19317437<ref>PMID:19317437</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 3gmc" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 700743]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Begley, T P]]
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[[Category: Mesorhizobium loti]]
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[[Category: Ealick, S E]]
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[[Category: Begley TP]]
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[[Category: McCulloch, K M]]
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[[Category: Ealick SE]]
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[[Category: Mukherjee, T]]
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[[Category: McCulloch KM]]
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[[Category: Flavin monooxygenase]]
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[[Category: Mukherjee T]]
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[[Category: Oxidoreductase]]
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Current revision

Crystal Structure of 2-Methyl-3-hydroxypyridine-5-carboxylic acid Oxygenase with substrate bound

PDB ID 3gmc

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