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3q2o
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| - | [[ | + | ==Crystal Structure of purK: N5-carboxyaminoimidazole ribonucleotide synthetase== |
| + | <StructureSection load='3q2o' size='340' side='right' caption='[[3q2o]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3q2o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_anthracis Bacillus anthracis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q2O FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAA_0344, purK ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoribosylaminoimidazole_carboxylase Phosphoribosylaminoimidazole carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.21 4.1.1.21] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q2o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q2o RCSB], [http://www.ebi.ac.uk/pdbsum/3q2o PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The apo structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis (baPurK) with Mg2+ in the active site is reported at 1.96 A resolution. PurK is an enzyme in the purine-biosynthetic pathway, unique to prokaryotes, that converts 5-aminoimidazole ribonucleotide to N5-carboxyaminoimidazole ribonucleotide and has been suggested as a potential antimicrobial drug target. Two interesting features of baPurK are a flexible B-loop (residues 149/150-157) that is in close contact with the active site and the binding of Mg2+ to the active site without additional ligands. | ||
| - | + | Structure of N5-carboxyaminoimidazole ribonucleotide synthase (PurK) from Bacillus anthracis.,Tuntland ML, Johnson ME, Fung LW, Santarsiero BD Acta Crystallogr D Biol Crystallogr. 2011 Oct;67(Pt 10):870-4. Epub 2011, Sep 8. PMID:21931218<ref>PMID:21931218</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
| - | < | + | |
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Phosphoribosylaminoimidazole carboxylase]] | [[Category: Phosphoribosylaminoimidazole carboxylase]] | ||
Revision as of 05:27, 4 June 2014
Crystal Structure of purK: N5-carboxyaminoimidazole ribonucleotide synthetase
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