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==Crystal Structure of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis str. Ames==
==Crystal Structure of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis str. Ames==
<StructureSection load='3tsb' size='340' side='right' caption='[[3tsb]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
<StructureSection load='3tsb' size='340' side='right'caption='[[3tsb]], [[Resolution|resolution]] 2.59&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tsb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis_(strain_ames) Bacillus anthracis (strain ames)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TSB FirstGlance]. <br>
<table><tr><td colspan='2'>[[3tsb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_anthracis_str._Ames Bacillus anthracis str. Ames]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TSB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.595&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">guaB, BAS0011, BA_0008, GBAA_0008 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=198094 Bacillus anthracis (strain Ames)])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=3tsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsb OCA], [https://pdbe.org/3tsb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tsb RCSB], [https://www.ebi.ac.uk/pdbsum/3tsb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsb 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=3tsb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tsb OCA], [http://pdbe.org/3tsb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tsb RCSB], [http://www.ebi.ac.uk/pdbsum/3tsb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tsb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q81W29_BACAN Q81W29_BACAN]] 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/A0A6L8P2U9_BACAN A0A6L8P2U9_BACAN] 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_01964]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Inosine 5'-monophosphate dehydrogenase (IMPDH) catalyzes the first unique step of the GMP branch of the purine nucleotide biosynthetic pathway. This enzyme is found in organisms of all three kingdoms. IMPDH inhibitors have broad clinical applications in cancer treatment, as antiviral drugs and as immunosuppressants, and have also displayed antibiotic activity. We have determined three crystal structures of Bacillus anthracis IMPDH, in a phosphate ion-bound (termed "apo") form and in complex with its substrate, inosine 5'-monophosphate (IMP), and product, xanthosine 5'-monophosphate (XMP). This is the first example of a bacterial IMPDH in more than one state from the same organism. Furthermore, for the first time for a prokaryotic enzyme, the entire active site flap, containing the conserved Arg-Tyr dyad, is clearly visible in the structure of the apoenzyme. Kinetic parameters for the enzymatic reaction were also determined, and the inhibitory effect of XMP and mycophenolic acid (MPA) has been studied. In addition, the inhibitory potential of two known Cryptosporidium parvum IMPDH inhibitors was examined for the B. anthracis enzyme and compared with those of three bacterial IMPDHs from Campylobacter jejuni, Clostridium perfringens, and Vibrio cholerae. The structures contribute to the characterization of the active site and design of inhibitors that specifically target B. anthracis and other microbial IMPDH enzymes.
 
Bacillus anthracis inosine 5'-monophosphate dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate-, and product-bound complexes.,Makowska-Grzyska M, Kim Y, Wu R, Wilton R, Gollapalli DR, Wang XK, Zhang R, Jedrzejczak R, Mack JC, Maltseva N, Mulligan R, Binkowski TA, Gornicki P, Kuhn ML, Anderson WF, Hedstrom L, Joachimiak A Biochemistry. 2012 Aug 7;51(31):6148-63. Epub 2012 Jul 25. PMID:22788966<ref>PMID:22788966</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tsb" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Inosine monophosphate dehydrogenase|Inosine monophosphate dehydrogenase]]
*[[Inosine monophosphate dehydrogenase 3D structures|Inosine monophosphate dehydrogenase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: IMP dehydrogenase]]
[[Category: Bacillus anthracis str. Ames]]
[[Category: Structural genomic]]
[[Category: Large Structures]]
[[Category: Hasseman, J]]
[[Category: Anderson WF]]
[[Category: Joachimiak, A]]
[[Category: Hasseman J]]
[[Category: Kim, Y]]
[[Category: Joachimiak A]]
[[Category: Makowska-Grzyska, M]]
[[Category: Kim Y]]
[[Category: Cbs-domain]]
[[Category: Makowska-Grzyska M]]
[[Category: Csgid]]
[[Category: Cytosol]]
[[Category: Oxidoreductase]]
[[Category: Tim-barrel]]

Latest revision as of 16:37, 14 March 2024

Crystal Structure of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis str. AmesCrystal Structure of Inosine-5'-monophosphate Dehydrogenase from Bacillus anthracis str. Ames

Structural highlights

3tsb is a 2 chain structure with sequence from Bacillus anthracis str. Ames. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.595Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A6L8P2U9_BACAN 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_01964]

See Also

3tsb, resolution 2.59Å

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