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3hfj

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Revision as of 12:46, 23 March 2022

Bacillus anthracis nicotinate mononucleotide adenylytransferase (nadD) in complex with inhibitor CID 3289443

Structural highlights

3hfj is a 2 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:	BAS4230, NadD ("Bacillus cereus var. anthracis" (Cohn 1872) Smith et al. 1946)
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

The emergence of multidrug-resistant pathogens necessitates the search for new antibiotics acting on previously unexplored targets. Nicotinate mononucleotide adenylyltransferase of the NadD family, an essential enzyme of NAD biosynthesis in most bacteria, was selected as a target for structure-based inhibitor development. Using iterative in silico and in vitro screens, we identified small molecule compounds that efficiently inhibited target enzymes from Escherichia coli (ecNadD) and Bacillus anthracis (baNadD) but had no effect on functionally equivalent human enzymes. On-target antibacterial activity was demonstrated for some of the selected inhibitors. A 3D structure of baNadD was solved in complex with one of these inhibitors (3_02), providing mechanistic insights and guidelines for further improvement. Most importantly, the results of this study help validate NadD as a target for the development of antibacterial agents with potential broad-spectrum activity.

Targeting NAD biosynthesis in bacterial pathogens: Structure-based development of inhibitors of nicotinate mononucleotide adenylyltransferase NadD.,Sorci L, Pan Y, Eyobo Y, Rodionova I, Huang N, Kurnasov O, Zhong S, MacKerell AD Jr, Zhang H, Osterman AL Chem Biol. 2009 Aug 28;16(8):849-61. PMID:19716475^[1]

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

References

↑ Sorci L, Pan Y, Eyobo Y, Rodionova I, Huang N, Kurnasov O, Zhong S, MacKerell AD Jr, Zhang H, Osterman AL. Targeting NAD biosynthesis in bacterial pathogens: Structure-based development of inhibitors of nicotinate mononucleotide adenylyltransferase NadD. Chem Biol. 2009 Aug 28;16(8):849-61. PMID:19716475 doi:10.1016/j.chembiol.2009.07.006

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/3hfj"

@@ Line 1: / Line 1: @@
 ==Bacillus anthracis nicotinate mononucleotide adenylytransferase (nadD) in complex with inhibitor CID 3289443==
-<StructureSection load='3hfj' size='340' side='right' caption='[[3hfj]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
+<StructureSection load='3hfj' size='340' side='right'caption='[[3hfj]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3hfj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"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 [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HFJ FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3hfj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"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 [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HFJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HFJ FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DZ9:3-AMINO-N-(3-FLUOROPHENYL)-6-THIOPHEN-2-YLTHIENO[2,3-B]PYRIDINE-2-CARBOXAMIDE'>DZ9</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DZ9:3-AMINO-N-(3-FLUOROPHENYL)-6-THIOPHEN-2-YLTHIENO[2,3-B]PYRIDINE-2-CARBOXAMIDE'>DZ9</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS4230, 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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAS4230, NadD ([https://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='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=3hfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfj OCA], [http://pdbe.org/3hfj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3hfj RCSB], [http://www.ebi.ac.uk/pdbsum/3hfj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfj 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=3hfj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hfj OCA], [https://pdbe.org/3hfj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hfj RCSB], [https://www.ebi.ac.uk/pdbsum/3hfj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hfj ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/Q6HT60_BACAN Q6HT60_BACAN]] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity).[HAMAP-Rule:MF_00244]
+[[https://www.uniprot.org/uniprot/Q6HT60_BACAN Q6HT60_BACAN]] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD) (By similarity).[HAMAP-Rule:MF_00244]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 33: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Eyobo, Y]]
 [[Category: Huang, N]]

3hfj

From Proteopedia

Revision as of 12:46, 23 March 2022

Bacillus anthracis nicotinate mononucleotide adenylytransferase (nadD) in complex with inhibitor CID 3289443

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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