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| | <StructureSection load='4qf5' size='340' side='right'caption='[[4qf5]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4qf5' size='340' side='right'caption='[[4qf5]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qf5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Acib3 Acib3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QF5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QF5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qf5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii_AB307-0294 Acinetobacter baumannii AB307-0294]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QF5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QF5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qdi|4qdi]]</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=4qf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qf5 OCA], [https://pdbe.org/4qf5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qf5 RCSB], [https://www.ebi.ac.uk/pdbsum/4qf5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qf5 ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABBFA_000315 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=557600 ACIB3])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine_ligase UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.2.10 6.3.2.10] </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=4qf5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qf5 OCA], [http://pdbe.org/4qf5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qf5 RCSB], [http://www.ebi.ac.uk/pdbsum/4qf5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qf5 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/B7GVN5_ACIB3 B7GVN5_ACIB3]] Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.[RuleBase:RU004136] | + | [https://www.uniprot.org/uniprot/A0A0J9X1Z8_ACIB3 A0A0J9X1Z8_ACIB3] Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.[HAMAP-Rule:MF_02019][RuleBase:RU004136] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acib3]] | + | [[Category: Acinetobacter baumannii AB307-0294]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase]]
| + | [[Category: An YJ]] |
| - | [[Category: An, Y J]] | + | [[Category: Cha SS]] |
| - | [[Category: Cha, S S]] | + | [[Category: Jeong CS]] |
| - | [[Category: Jeong, C S]] | + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Murf]]
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| - | [[Category: Udp-n-acetylmuramoyl-tripeptide-d-alanyl-d-ananine ligase]]
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| Structural highlights
Function
A0A0J9X1Z8_ACIB3 Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.[HAMAP-Rule:MF_02019][RuleBase:RU004136]
Publication Abstract from PubMed
MurF adds d-Ala-d-Ala dipeptide to UDP-N-acetylmuramyl-l-Ala-gamma-d-Glu-m-DAP (or l-Lys) in an ATP-dependent manner, which is the last step in the biosynthesis of monomeric precursor of peptidoglycan. Here we report crystal structures of two MurF-ATP complexes: the MurF-ATP complex and the MurF-ATP-UDP complex. The ATP-binding mode revealed by the crystal structure of the MurF-ATP complex confirms the previous biochemical demonstration that a carbamoylated lysine and two Mg(2+) ions are required for enzyme activity of MurF. The UDP-MurF interactions observed in the crystal structure of the MurF-ATP-UDP complex depict the characteristic substrate-binding mode of MurF. The emergence and dissemination of multidrug-resistant Acinetobacter baumannii strains are great threats to public health. Therefore, the structural information on A. baumannii MurF as a validated target for drug discovery will provide a framework to develop antibacterial agents against multidrug-resistant A. baumannii infections as well as to understand the reaction mechanism of MurF.
ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF.,Cha SS, An YJ, Jeong CS, Yu JH, Chung KM Biochem Biophys Res Commun. 2014 Jul 25;450(2):1045-50. doi:, 10.1016/j.bbrc.2014.06.108. Epub 2014 Jun 27. PMID:24978312[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Cha SS, An YJ, Jeong CS, Yu JH, Chung KM. ATP-binding mode including a carbamoylated lysine and two Mg(2+) ions, and substrate-binding mode in Acinetobacter baumannii MurF. Biochem Biophys Res Commun. 2014 Jul 25;450(2):1045-50. doi:, 10.1016/j.bbrc.2014.06.108. Epub 2014 Jun 27. PMID:24978312 doi:http://dx.doi.org/10.1016/j.bbrc.2014.06.108
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