|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5ahl' size='340' side='right'caption='[[5ahl]], [[Resolution|resolution]] 1.95Å' scene=''> | | <StructureSection load='5ahl' size='340' side='right'caption='[[5ahl]], [[Resolution|resolution]] 1.95Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ahl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseae Pseae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AHL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5AHL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ahl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa_PAO1 Pseudomonas aeruginosa PAO1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5AHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5AHL FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ahm|5ahm]], [[5ahn|5ahn]]</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=5ahl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ahl OCA], [https://pdbe.org/5ahl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ahl RCSB], [https://www.ebi.ac.uk/pdbsum/5ahl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ahl ProSAT]</span></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='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=5ahl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ahl OCA], [http://pdbe.org/5ahl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ahl RCSB], [http://www.ebi.ac.uk/pdbsum/5ahl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ahl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q9HXM5_PSEAE Q9HXM5_PSEAE]] 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 (By similarity).[HAMAP-Rule:MF_01964] | + | [https://www.uniprot.org/uniprot/Q9HXM5_PSEAE Q9HXM5_PSEAE] 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 (By similarity).[HAMAP-Rule:MF_01964] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 27: |
Line 25: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: IMP dehydrogenase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Alexandre, T]] | + | [[Category: Alexandre T]] |
| - | [[Category: Gelin, M]] | + | [[Category: Gelin M]] |
| - | [[Category: Haouz, A]] | + | [[Category: Haouz A]] |
| - | [[Category: Labesse, G]] | + | [[Category: Labesse G]] |
| - | [[Category: Munier-Lehmann, H]] | + | [[Category: Munier-Lehmann H]] |
| - | [[Category: Allosteric regu nucleotide metabolism]]
| + | |
| - | [[Category: Cbs module]]
| + | |
| - | [[Category: Deletion mutant]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
Q9HXM5_PSEAE 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 (By similarity).[HAMAP-Rule:MF_01964]
Publication Abstract from PubMed
Inosine-5'-monophosphate dehydrogenases (IMPDHs), which are the rate-limiting enzymes in guanosine-nucleotide biosynthesis, are important therapeutic targets. Despite in-depth functional and structural characterizations of various IMPDHs, the role of the Bateman domain containing two CBS motifs remains controversial. Their involvement in the allosteric regulation of Pseudomonas aeruginosa IMPDH by Mg-ATP has recently been reported. To better understand the function of IMPDH and the importance of the CBS motifs, the structure of a variant devoid of these modules (DeltaCBS) was solved at high resolution in the apo form and in complex with IMP. In addition, a single amino-acid substitution variant, D199N, was also structurally characterized: the mutation corresponds to the autosomal dominant mutant D226N of human IMPDH1, which is responsible for the onset of the retinopathy adRP10. These new structures shed light onto the possible mechanism of regulation of the IMPDH enzymatic activity. In particular, three conserved loops seem to be key players in this regulation as they connect the tetramer-tetramer interface with the active site and show significant modification upon substrate binding.
Crystallographic studies of two variants of Pseudomonas aeruginosa IMPDH with impaired allosteric regulation.,Labesse G, Alexandre T, Gelin M, Haouz A, Munier-Lehmann H Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1890-9. doi:, 10.1107/S1399004715013115. Epub 2015 Aug 25. PMID:26327379[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Labesse G, Alexandre T, Gelin M, Haouz A, Munier-Lehmann H. Crystallographic studies of two variants of Pseudomonas aeruginosa IMPDH with impaired allosteric regulation. Acta Crystallogr D Biol Crystallogr. 2015 Sep 1;71(Pt 9):1890-9. doi:, 10.1107/S1399004715013115. Epub 2015 Aug 25. PMID:26327379 doi:http://dx.doi.org/10.1107/S1399004715013115
|
