This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3dv2

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:57, 25 October 2017

Crystal Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis

Structural highlights

3dv2 is a 4 chain structure with sequence from "bacillus_cereus_var._anthracis"_(cohn_1872)_smith_et_al._1946 "bacillus cereus var. anthracis" (cohn 1872) smith et al. 1946. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	nadD ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946)
Activity:	Nicotinate-nucleotide adenylyltransferase, with EC number 2.7.7.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q6HT60_BACAN] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity).[HAMAP-Rule:MF_00244]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lu S, Smith CD, Yang Z, Pruett PS, Nagy L, McCombs D, Delucas LJ, Brouillette WJ, Brouillette CG. Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Oct 1;64(Pt, 10):893-8. Epub 2008 Sep 30. PMID:18931430 doi:10.1107/S1744309108029102

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3dv2"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis==
 <StructureSection load='3dv2' size='340' side='right' caption='[[3dv2]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <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 cereus var. anthracis" (Cohn 1872) Smith et al. 1946])</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://pdbe.org/3dv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dv2 RCSB], [http://www.ebi.ac.uk/pdbsum/3dv2 PDBsum]</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://pdbe.org/3dv2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3dv2 RCSB], [http://www.ebi.ac.uk/pdbsum/3dv2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3dv2 ProSAT]</span></td></tr>
 </table>
 == Function ==

3dv2

From Proteopedia

Revision as of 08:57, 25 October 2017

Crystal Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox