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| | ==Crystal structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase== | | ==Crystal structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase== |
| - | <StructureSection load='3zfh' size='340' side='right' caption='[[3zfh]], [[Resolution|resolution]] 2.25Å' scene=''> | + | <StructureSection load='3zfh' size='340' side='right'caption='[[3zfh]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3zfh]] 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=3ZFH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZFH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3zfh]] 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=3ZFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZFH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 2.25Å</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=CL:CHLORIDE+ION'>CL</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=3zfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zfh OCA], [http://pdbe.org/3zfh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zfh RCSB], [http://www.ebi.ac.uk/pdbsum/3zfh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zfh 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=3zfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zfh OCA], [https://pdbe.org/3zfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zfh RCSB], [https://www.ebi.ac.uk/pdbsum/3zfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zfh 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 == |
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| | ==See Also== | | ==See Also== |
| - | *[[Inosine monophosphate dehydrogenase|Inosine monophosphate dehydrogenase]] | + | *[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: IMP dehydrogenase]] | + | [[Category: Large Structures]] |
| - | [[Category: Pseae]] | + | [[Category: Pseudomonas aeruginosa PAO1]] |
| - | [[Category: Hunter, W N]] | + | [[Category: Hunter WN]] |
| - | [[Category: Owen, R]] | + | [[Category: Owen R]] |
| - | [[Category: Rao, V A]] | + | [[Category: Rao VA]] |
| - | [[Category: Shepherd, S M]] | + | [[Category: Shepherd SM]] |
| - | [[Category: Guanine nucleotide biosynthesis]]
| + | |
| - | [[Category: Oxidoreductase]]
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| 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 dehydrogenase (IMPDH) represents a potential antimicrobial drug target. The crystal structure of recombinant Pseudomonas aeruginosa IMPDH has been determined to a resolution of 2.25 A. The structure is a homotetramer of subunits dominated by a (beta/alpha)8-barrel fold, consistent with other known structures of IMPDH. Also in common with previous work, the cystathionine beta-synthase domains, residues 92-204, are not present in the model owing to disorder. However, unlike the majority of available structures, clearly defined electron density exists for a loop that creates part of the active site. This loop, composed of residues 297-315, links alpha8 and beta9 and carries the catalytic Cys304. P. aeruginosa IMPDH shares a high level of sequence identity with bacterial and protozoan homologues, with residues involved in binding substrate and the NAD(+) cofactor being conserved. Specific differences that have been proven to contribute to selectivity against the human enzyme in a study of Cryptosporidium parvum IMPDH are also conserved, highlighting the potential value of IMPDH as a drug target.
Structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase.,Rao VA, Shepherd SM, Owen R, Hunter WN Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):243-7. doi:, 10.1107/S1744309113002352. Epub 2013 Feb 22. PMID:23519796[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Rao VA, Shepherd SM, Owen R, Hunter WN. Structure of Pseudomonas aeruginosa inosine 5'-monophosphate dehydrogenase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Mar 1;69(Pt 3):243-7. doi:, 10.1107/S1744309113002352. Epub 2013 Feb 22. PMID:23519796 doi:http://dx.doi.org/10.1107/S1744309113002352
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