4ojv: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4ojv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OJV FirstGlance]. <br>
<table><tr><td colspan='2'>[[4ojv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OJV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OJV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.31&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4ojv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojv OCA], [https://pdbe.org/4ojv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ojv RCSB], [https://www.ebi.ac.uk/pdbsum/4ojv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ojv ProSAT]</span></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=4ojv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ojv OCA], [https://pdbe.org/4ojv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ojv RCSB], [https://www.ebi.ac.uk/pdbsum/4ojv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ojv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/PDE1_YEAST PDE1_YEAST] Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).
[https://www.uniprot.org/uniprot/PDE1_YEAST PDE1_YEAST] Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cyclic nucleotide phosphodiesterases (PDEs) decompose second messengers cAMP and cGMP that play critical roles in many physiological processes. PDE1 of Saccharomyces cerevisiae has been subcloned and expressed in Escherichia coli. Recombinant yPDE1 has a KM of 110 muM and a kcat of 16.9 s(-1) for cAMP and a KM of 105 muM and a kcat of 11.8 s(-1) for cGMP. Thus, the specificity constant (kcat/KM(cAMP))/(kcat/KM(cGMP)) of 1.4 indicates a dual specificity of yPDE1 for hydrolysis of both cAMP and cGMP. The crystal structures of unliganded yPDE1 and its complex with GMP at 1.31 A resolution reveal a new structural folding that is different from those of human PDEs but is partially similar to that of some other metalloenzymes such as metallo-beta-lactamase. In spite of their different structures and divalent metals, yPDE1 and human PDEs may share a common mechanism for hydrolysis of cAMP and cGMP.
Dual specificity and novel structural folding of yeast phosphodiesterase-1 for hydrolysis of second messengers cyclic adenosine and guanosine 3',5'-monophosphate.,Tian Y, Cui W, Huang M, Robinson H, Wan Y, Wang Y, Ke H Biochemistry. 2014 Aug 5;53(30):4938-45. doi: 10.1021/bi500406h. Epub 2014 Jul, 22. PMID:25050706<ref>PMID:25050706</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ojv" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 15:40, 1 March 2024

Crystal structure of unliganded yeast PDE1Crystal structure of unliganded yeast PDE1

Structural highlights

4ojv is a 1 chain structure with sequence from Saccharomyces cerevisiae S288C. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.31Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDE1_YEAST Controls the level of cAMP in yeast cells, together with the high-affinity cAMP phosphodiesterase (PDE2).

See Also

4ojv, resolution 1.31Å

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