3dv2
From Proteopedia
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- | [[ | + | ==Crystal Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis== |
+ | <StructureSection load='3dv2' size='340' side='right' caption='[[3dv2]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3dv2]] is a 4 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=3DV2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3DV2 FirstGlance]. <br> | ||
+ | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nadD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1392 Bacillus anthracis])</td></tr> | ||
+ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Nicotinate-nucleotide_adenylyltransferase Nicotinate-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.18 2.7.7.18] </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=3dv2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dv2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dv2 RCSB], [http://www.ebi.ac.uk/pdbsum/3dv2 PDBsum]</span></td></tr> | ||
+ | </table> | ||
+ | == Evolutionary Conservation == | ||
+ | [[Image:Consurf_key_small.gif|200px|right]] | ||
+ | Check<jmol> | ||
+ | <jmolCheckbox> | ||
+ | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dv/3dv2_consurf.spt"</scriptWhenChecked> | ||
+ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
+ | <text>to colour the structure by Evolutionary Conservation</text> | ||
+ | </jmolCheckbox> | ||
+ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC 2.7.7.18) is the penultimate enzyme in the biosynthesis of NAD(+) and catalyzes the adenylation of nicotinic acid mononucleotide (NaMN) by ATP to form nicotinic acid adenine dinucleotide (NaAD). This enzyme is regarded as a suitable candidate for antibacterial drug development; as such, Bacillus anthracis NaMNAT (BA NaMNAT) was heterologously expressed in Escherichia coli for the purpose of inhibitor discovery and crystallography. The crystal structure of BA NaMNAT was determined by molecular replacement, revealing two dimers per asymmetric unit, and was refined to an R factor and R(free) of 0.228 and 0.263, respectively, at 2.3 A resolution. The structure is very similar to that of B. subtilis NaMNAT (BS NaMNAT), which is also a dimer, and another independently solved structure of BA NaMNAT recently released from the PDB along with two ligated forms. Comparison of these and other less related bacterial NaMNAT structures support the presence of considerable conformational heterogeneity and flexibility in three loops surrounding the substrate-binding area. | ||
- | + | Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis.,Lu S, Smith CD, Yang Z, Pruett PS, Nagy L, McCombs D, Delucas LJ, Brouillette WJ, Brouillette CG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt, 10):893-8. Epub 2008 Sep 30. PMID:18931430<ref>PMID:18931430</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
+ | </div> | ||
- | + | ==See Also== | |
- | + | *[[P73|P73]] | |
- | == | + | == References == |
- | [[ | + | <references/> |
- | + | __TOC__ | |
- | == | + | </StructureSection> |
- | < | + | |
[[Category: Bacillus anthracis]] | [[Category: Bacillus anthracis]] | ||
[[Category: Nicotinate-nucleotide adenylyltransferase]] | [[Category: Nicotinate-nucleotide adenylyltransferase]] | ||
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[[Category: Nucleotidyltransferase]] | [[Category: Nucleotidyltransferase]] | ||
[[Category: Pyridine nucleotide biosynthesis]] | [[Category: Pyridine nucleotide biosynthesis]] | ||
- | [[Category: | + | [[Category: Rossmann fold]] |
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 14:25, 3 November 2014
Crystal Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis
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Categories: Bacillus anthracis | Nicotinate-nucleotide adenylyltransferase | Brouillette, C G. | Brouillette, W J. | DeLucas, L J. | Lu, S. | McCombs, D P. | Nagy, L. | Pruett, P S. | Smith, C D. | Yang, Z. | Alpha and beta protein | Nad | Nucleotidyltransferase | Pyridine nucleotide biosynthesis | Rossmann fold | Transferase