6cpu: Difference between revisions
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<StructureSection load='6cpu' size='340' side='right'caption='[[6cpu]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='6cpu' size='340' side='right'caption='[[6cpu]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6cpu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11006_[[ | <table><tr><td colspan='2'>[[6cpu]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11006_[[monilia_stellatoidea]] Atcc 11006 [[monilia stellatoidea]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CPU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CPU FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PDE2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5476 ATCC 11006 [[Monilia stellatoidea]]])</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=6cpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpu OCA], [http://pdbe.org/6cpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpu RCSB], [http://www.ebi.ac.uk/pdbsum/6cpu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpu ProSAT]</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=6cpu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cpu OCA], [http://pdbe.org/6cpu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6cpu RCSB], [http://www.ebi.ac.uk/pdbsum/6cpu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6cpu ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The cAMP signaling system plays important roles in the physiological processes of pathogen yeast Candida albicans, but its functional mechanism has not been well illustrated. Here, we report the enzymatic characterization and crystal structures of C. albicans phosphodiesterase 2 (caPDE2) in the unliganded and 3-isobutyl-1-methylxanthine-complexed forms. caPDE2 is a monomer in liquid and crystal states and specifically hydrolyzes cAMP with a KM of 35 nM. It does not effectively hydrolyze cGMP as shown by the 1.32 x 10(5)-fold specificity of cAMP/cGMP. The crystal structure of caPDE2 shows significant differences from those of human PDEs. First, the N-terminal fragment of caPDE2 (residues 1-201) tightly associates with the catalytic domain to form a rigid molecular entity, implying its stable molecular conformation for C. albicans to resist environmental stresses. Second, the M-loop, a critical fragment for binding of the substrate and inhibitors to human PDEs, is not a part of the caPDE2 active site. This feature of caPDE2 may provide a structural basis for the design of selective inhibitors for the treatment of yeast infection. | |||
Crystal Structures of Candida albicans Phosphodiesterase 2 and Implications for Its Biological Functions.,Yao T, Huang Y, Zhang M, Chen Y, Pei H, Shi J, Wang H, Wang Y, Ke H Biochemistry. 2018 Oct 23;57(42):6070-6077. doi: 10.1021/acs.biochem.8b00707., Epub 2018 Oct 4. PMID:30231198<ref>PMID:30231198</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6cpu" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 13:49, 1 January 2020
Crystal structure of yeast caPDE2Crystal structure of yeast caPDE2
Structural highlights
Publication Abstract from PubMedThe cAMP signaling system plays important roles in the physiological processes of pathogen yeast Candida albicans, but its functional mechanism has not been well illustrated. Here, we report the enzymatic characterization and crystal structures of C. albicans phosphodiesterase 2 (caPDE2) in the unliganded and 3-isobutyl-1-methylxanthine-complexed forms. caPDE2 is a monomer in liquid and crystal states and specifically hydrolyzes cAMP with a KM of 35 nM. It does not effectively hydrolyze cGMP as shown by the 1.32 x 10(5)-fold specificity of cAMP/cGMP. The crystal structure of caPDE2 shows significant differences from those of human PDEs. First, the N-terminal fragment of caPDE2 (residues 1-201) tightly associates with the catalytic domain to form a rigid molecular entity, implying its stable molecular conformation for C. albicans to resist environmental stresses. Second, the M-loop, a critical fragment for binding of the substrate and inhibitors to human PDEs, is not a part of the caPDE2 active site. This feature of caPDE2 may provide a structural basis for the design of selective inhibitors for the treatment of yeast infection. Crystal Structures of Candida albicans Phosphodiesterase 2 and Implications for Its Biological Functions.,Yao T, Huang Y, Zhang M, Chen Y, Pei H, Shi J, Wang H, Wang Y, Ke H Biochemistry. 2018 Oct 23;57(42):6070-6077. doi: 10.1021/acs.biochem.8b00707., Epub 2018 Oct 4. PMID:30231198[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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