2g4o: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2g4o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G4O FirstGlance]. <br> | <table><tr><td colspan='2'>[[2g4o]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G4O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2G4O FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </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=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g4h|2g4h]], [[2g4i|2g4i]], [[2g4j|2g4j]], [[2g4k|2g4k]], [[2g4l|2g4l]], [[2g4m|2g4m]], [[2g4n|2g4n]], [[2g4p|2g4p]], [[2g4q|2g4q]], [[2g4r|2g4r]], [[2g4s|2g4s]], [[2g4t|2g4t]], [[2g4u|2g4u]], [[2g4v|2g4v]], [[2g4w|2g4w]], [[2g4x|2g4x]], [[2g4y|2g4y]], [[2g4z|2g4z]], [[2g51|2g51]], [[2g52|2g52]], [[2g55|2g55]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g4h|2g4h]], [[2g4i|2g4i]], [[2g4j|2g4j]], [[2g4k|2g4k]], [[2g4l|2g4l]], [[2g4m|2g4m]], [[2g4n|2g4n]], [[2g4p|2g4p]], [[2g4q|2g4q]], [[2g4r|2g4r]], [[2g4s|2g4s]], [[2g4t|2g4t]], [[2g4u|2g4u]], [[2g4v|2g4v]], [[2g4w|2g4w]], [[2g4x|2g4x]], [[2g4y|2g4y]], [[2g4z|2g4z]], [[2g51|2g51]], [[2g52|2g52]], [[2g55|2g55]]</td></tr> | ||
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">leuB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2g4o RCSB], [http://www.ebi.ac.uk/pdbsum/2g4o PDBsum]</span></td></tr> | <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=2g4o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2g4o RCSB], [http://www.ebi.ac.uk/pdbsum/2g4o PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/LEU3_MYCTU LEU3_MYCTU]] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01035] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: 3-isopropylmalate dehydrogenase]] | [[Category: 3-isopropylmalate dehydrogenase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Mueller-Dieckmann, C | [[Category: Mueller-Dieckmann, C]] | ||
[[Category: Weiss, M S | [[Category: Weiss, M S]] | ||
[[Category: Anomalous substructure of 3-isopropylmalate dehydrogenase]] | [[Category: Anomalous substructure of 3-isopropylmalate dehydrogenase]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 22:26, 24 December 2014
anomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASEanomalous substructure of 3-ISOPROPYLMALATE DEHYDROGENASE
Structural highlights
Function[LEU3_MYCTU] Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.[HAMAP-Rule:MF_01035] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set. On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.,Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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