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4z87

From Proteopedia

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Current revision

Structure of the IMP dehydrogenase from Ashbya gossypii bound to GDP

Structural highlights

4z87 is a 4 chain structure with sequence from Eremothecium gossypii ATCC 10895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.25Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q756Z6_ASHGO Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_03156]

Publication Abstract from PubMed

Inosine-5'-monophosphate dehydrogenase (IMPDH) plays key roles in purine nucleotide metabolism and cell proliferation. Although IMPDH is a widely studied therapeutic target, there is limited information about its physiological regulation. Using Ashbya gossypii as a model, we describe the molecular mechanism and the structural basis for the allosteric regulation of IMPDH by guanine nucleotides. We report that GTP and GDP bind to the regulatory Bateman domain, inducing octamers with compromised catalytic activity. Our data suggest that eukaryotic and prokaryotic IMPDHs might have developed different regulatory mechanisms, with GTP/GDP inhibiting only eukaryotic IMPDHs. Interestingly, mutations associated with human retinopathies map into the guanine nucleotide-binding sites including a previously undescribed non-canonical site and disrupt allosteric inhibition. Together, our results shed light on the mechanisms of the allosteric regulation of enzymes mediated by Bateman domains and provide a molecular basis for certain retinopathies, opening the door to new therapeutic approaches.

Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases.,Buey RM, Ledesma-Amaro R, Velazquez-Campoy A, Balsera M, Chagoyen M, de Pereda JM, Revuelta JL Nat Commun. 2015 Nov 12;6:8923. doi: 10.1038/ncomms9923. PMID:26558346^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Buey RM, Ledesma-Amaro R, Velazquez-Campoy A, Balsera M, Chagoyen M, de Pereda JM, Revuelta JL. Guanine nucleotide binding to the Bateman domain mediates the allosteric inhibition of eukaryotic IMP dehydrogenases. Nat Commun. 2015 Nov 12;6:8923. doi: 10.1038/ncomms9923. PMID:26558346 doi:http://dx.doi.org/10.1038/ncomms9923

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4z87"

Categories: Eremothecium gossypii ATCC 10895 | Large Structures | Buey RM | Revuelta JL | De Pereda JM

@@ Line 1: / Line 1: @@
 ==Structure of the IMP dehydrogenase from Ashbya gossypii bound to GDP==
-<StructureSection load='4z87' size='340' side='right' caption='[[4z87]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+<StructureSection load='4z87' size='340' side='right'caption='[[4z87]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4z87]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Z87 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4z87]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eremothecium_gossypii_ATCC_10895 Eremothecium gossypii ATCC 10895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z87 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z87 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</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]] 2.25&#8491;</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/IMP_dehydrogenase IMP dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.205 1.1.1.205] </span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5GP:GUANOSINE-5-MONOPHOSPHATE'>5GP</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=4z87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z87 OCA], [http://pdbe.org/4z87 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4z87 RCSB], [http://www.ebi.ac.uk/pdbsum/4z87 PDBsum]</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=4z87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z87 OCA], [https://pdbe.org/4z87 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z87 RCSB], [https://www.ebi.ac.uk/pdbsum/4z87 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z87 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q756Z6_ASHGO Q756Z6_ASHGO]] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_03156]
+[https://www.uniprot.org/uniprot/Q756Z6_ASHGO Q756Z6_ASHGO] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.[HAMAP-Rule:MF_03156]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 4z87" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: IMP dehydrogenase]]
+[[Category: Eremothecium gossypii ATCC 10895]]
-[[Category: Buey, R M]]
+[[Category: Large Structures]]
-[[Category: Pereda, J M.de]]
+[[Category: Buey RM]]
-[[Category: Revuelta, J L]]
+[[Category: Revuelta JL]]
-[[Category: Bateman domain]]
+[[Category: De Pereda JM]]
-[[Category: Imp dehydrgoenase]]
-[[Category: Oxidoreductase]]

4z87

From Proteopedia

Current revision

Structure of the IMP dehydrogenase from Ashbya gossypii bound to GDP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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