5cef: Difference between revisions
New page: '''Unreleased structure''' The entry 5cef is ON HOLD Authors: Dahal, G.P., Viola, R.E. Description: Cystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoforman... |
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The | ==Cystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans== | ||
<StructureSection load='5cef' size='340' side='right'caption='[[5cef]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5cef]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptococcus_neoformans_var._neoformans_JEC21 Cryptococcus neoformans var. neoformans JEC21]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5CEF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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=5cef FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cef OCA], [https://pdbe.org/5cef PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5cef RCSB], [https://www.ebi.ac.uk/pdbsum/5cef PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5cef ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5KPK7_CRYNJ Q5KPK7_CRYNJ] | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Dahal | <div class="pdbe-citations 5cef" style="background-color:#fffaf0;"></div> | ||
[[Category: Viola | |||
==See Also== | |||
*[[Aspartate-semialdehyde dehydrogenase 3D structures|Aspartate-semialdehyde dehydrogenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cryptococcus neoformans var. neoformans JEC21]] | |||
[[Category: Large Structures]] | |||
[[Category: Dahal GP]] | |||
[[Category: Viola RE]] | |||
Latest revision as of 11:37, 27 September 2023
Cystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoformansCystal structure of aspartate semialdehyde dehydrogenase from Cryptococcus neoformans
Structural highlights
FunctionPublication Abstract from PubMedAspartate 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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