3hsk
From Proteopedia
(Difference between revisions)
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| - | + | ==Crystal Structure of Aspartate Semialdehyde Dehydrogenase with NADP from Candida albicans== | |
| - | + | <StructureSection load='3hsk' size='340' side='right' caption='[[3hsk]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3hsk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HSK FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CaO19.1559, CaO19.9132, HOM2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 Candida albicans])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate-semialdehyde_dehydrogenase Aspartate-semialdehyde dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.11 1.2.1.11] </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=3hsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hsk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hsk RCSB], [http://www.ebi.ac.uk/pdbsum/3hsk PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/hs/3hsk_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The enzyme aspartate semialdehyde dehydrogenase (ASADH) catalyzes a critical transformation that produces the first branch-point intermediate in an essential microbial amino-acid biosynthetic pathway. The first structure of an ASADH isolated from a fungal species (Candida albicans) has been determined as a complex with its pyridine nucleotide cofactor. This enzyme is a functional dimer, with a similar overall fold and domain organization to the structurally characterized bacterial ASADHs. However, there are differences in the secondary-structural elements and in cofactor binding that are likely to cause the lower catalytic efficiency of this fungal enzyme. Alterations in the dimer interface, through deletion of a helical subdomain and replacement of amino acids that participate in a hydrogen-bonding network, interrupt the intersubunit-communication channels required to support an alternating-site catalytic mechanism. The detailed functional information derived from this new structure will allow an assessment of ASADH as a possible target for antifungal drug development. | ||
| - | + | Expansion of the aspartate beta-semialdehyde dehydrogenase family: the first structure of a fungal ortholog.,Arachea BT, Liu X, Pavlovsky AG, Viola RE Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):205-12. Epub 2010, Jan 22. PMID:20124701<ref>PMID:20124701</ref> | |
| - | + | ||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
==See Also== | ==See Also== | ||
*[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]] | *[[Aldehyde dehydrogenase|Aldehyde dehydrogenase]] | ||
*[[Aspartate-semialdehyde dehydrogenase|Aspartate-semialdehyde dehydrogenase]] | *[[Aspartate-semialdehyde dehydrogenase|Aspartate-semialdehyde dehydrogenase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Aspartate-semialdehyde dehydrogenase]] | [[Category: Aspartate-semialdehyde dehydrogenase]] | ||
[[Category: Candida albicans]] | [[Category: Candida albicans]] | ||
| - | [[Category: Arachea, B T | + | [[Category: Arachea, B T]] |
| - | [[Category: Liu, X | + | [[Category: Liu, X]] |
| - | [[Category: Pavlovsky, A | + | [[Category: Pavlovsky, A]] |
| - | [[Category: Viola, R E | + | [[Category: Viola, R E]] |
[[Category: Amino-acid biosynthesis]] | [[Category: Amino-acid biosynthesis]] | ||
[[Category: Aspartate semialdehyde dehydrogenase]] | [[Category: Aspartate semialdehyde dehydrogenase]] | ||
[[Category: Candida albicans nadp complex]] | [[Category: Candida albicans nadp complex]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
Revision as of 15:10, 18 December 2014
Crystal Structure of Aspartate Semialdehyde Dehydrogenase with NADP from Candida albicans
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