5bus: Difference between revisions

Line 6:

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bur|5bur]], [[5buq|5buq]]</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/o-succinylbenzoate--CoA_ligase o-succinylbenzoate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.26 6.2.1.26] </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=5bus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bus OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bus RCSB], [http://www.ebi.ac.uk/pdbsum/5bus 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=5bus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bus OCA], [http://pdbe.org/5bus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bus RCSB], [http://www.ebi.ac.uk/pdbsum/5bus PDBsum]</span></td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/MENE_BACSU MENE_BACSU]] Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).[HAMAP-Rule:MF_00731]

== Publication Abstract from PubMed ==

o-Succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme targeted for development of novel antibiotics in the menaquinone biosynthesis. Using its crystal structures in a ligand-free form or in complex with nucleotides, a conserved pattern is identified in the interaction between ATP and adenylating enzymes, including acyl/aryl-CoA synthetases, adenylation domains of nonribosomal peptide synthetases, and luciferases. It involves tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site. In MenE catalysis, this ATP-enzyme interaction creates a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling. In addition, the ATP-enzyme interaction is suggested to play a crucial catalytic role by mutation of the P-loop residues hydrogen-bonded to ATP. Moreover, the ATP-enzyme interaction has also clarified the positioning and catalytic role of a conserved lysine residue in stabilization of the transition state. These findings provide new insights into the adenylation half-reaction in the domain alteration catalytic mechanism of the adenylate-forming enzymes.

Structural Basis for the ATP-dependent Configuration of Adenylation Active Site in Bacillus subtilis o-Succinylbenzoyl-CoA Synthetase.,Chen Y, Sun Y, Song H, Guo Z J Biol Chem. 2015 Sep 25;290(39):23971-83. doi: 10.1074/jbc.M115.676304. Epub, 2015 Aug 14. PMID:26276389<ref>PMID:26276389</ref>

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

</div>

== References ==

__TOC__

</StructureSection>

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@@ Line 6: / Line 6: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bur|5bur]], [[5buq|5buq]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/o-succinylbenzoate--CoA_ligase o-succinylbenzoate--CoA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.2.1.26 6.2.1.26] </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=5bus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bus OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5bus RCSB], [http://www.ebi.ac.uk/pdbsum/5bus 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=5bus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bus OCA], [http://pdbe.org/5bus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bus RCSB], [http://www.ebi.ac.uk/pdbsum/5bus PDBsum]</span></td></tr>
 </table>
 == Function ==
 [[http://www.uniprot.org/uniprot/MENE_BACSU MENE_BACSU]] Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA).[HAMAP-Rule:MF_00731]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+o-Succinylbenzoyl-CoA synthetase, or MenE, is an essential adenylate-forming enzyme targeted for development of novel antibiotics in the menaquinone biosynthesis. Using its crystal structures in a ligand-free form or in complex with nucleotides, a conserved pattern is identified in the interaction between ATP and adenylating enzymes, including acyl/aryl-CoA synthetases, adenylation domains of nonribosomal peptide synthetases, and luciferases. It involves tight gripping interactions of the phosphate-binding loop (P-loop) with the ATP triphosphate moiety and an open-closed conformational change to form a compact adenylation active site. In MenE catalysis, this ATP-enzyme interaction creates a new binding site for the carboxylate substrate, allowing revelation of the determinants of substrate specificities and in-line alignment of the two substrates for backside nucleophilic substitution reaction by molecular modeling. In addition, the ATP-enzyme interaction is suggested to play a crucial catalytic role by mutation of the P-loop residues hydrogen-bonded to ATP. Moreover, the ATP-enzyme interaction has also clarified the positioning and catalytic role of a conserved lysine residue in stabilization of the transition state. These findings provide new insights into the adenylation half-reaction in the domain alteration catalytic mechanism of the adenylate-forming enzymes.
+Structural Basis for the ATP-dependent Configuration of Adenylation Active Site in Bacillus subtilis o-Succinylbenzoyl-CoA Synthetase.,Chen Y, Sun Y, Song H, Guo Z J Biol Chem. 2015 Sep 25;290(39):23971-83. doi: 10.1074/jbc.M115.676304. Epub, 2015 Aug 14. PMID:26276389<ref>PMID:26276389</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5bus" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>