5cef: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Cystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans==
+<StructureSection load='5cef' size='340' side='right' caption='[[5cef]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5cef]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CEF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CEF FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5cef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cef OCA], [http://pdbe.org/5cef PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cef RCSB], [http://www.ebi.ac.uk/pdbsum/5cef PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Aspartate semialdehyde dehydrogenase (ASADH) functions at a critical junction in the aspartate-biosynthetic pathway and represents a valid target for antimicrobial drug design. This enzyme catalyzes the NADPH-dependent reductive dephosphorylation of beta-aspartyl phosphate to produce the key intermediate aspartate semialdehyde. Production of this intermediate represents the first committed step in the biosynthesis of the essential amino acids methionine, isoleucine and threonine in fungi, and also the amino acid lysine in bacteria. The structure of a new fungal form of ASADH from Cryptococcus neoformans has been determined to 2.6 A resolution. The overall structure of CnASADH is similar to those of its bacterial orthologs, but with some critical differences both in biological assembly and in secondary-structural features that can potentially be exploited for the development of species-selective drugs.
-The entry 5cef is ON HOLD  until Paper Publication
+Structure of a fungal form of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans.,Dahal G, Viola RE Acta Crystallogr F Struct Biol Commun. 2015 Nov 1;71(Pt 11):1365-71. doi:, 10.1107/S2053230X15017495. Epub 2015 Oct 23. PMID:26527262<ref>PMID:26527262</ref>
-Authors: Dahal, G.P., Viola, R.E.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Cystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans
+<div class="pdbe-citations 5cef" style="background-color:#fffaf0;"></div>
-[[Category: Unreleased Structures]]
+== References ==
-[[Category: Dahal, G.P]]
+<references/>
-[[Category: Viola, R.E]]
+__TOC__
+</StructureSection>
+[[Category: Aspartate-semialdehyde dehydrogenase]]
+[[Category: Dahal, G P]]
+[[Category: Viola, R E]]
+[[Category: Oxidoreductase]]
+[[Category: Rossmann fold]]