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| | ==Crystal structure of MCAT from Streptococcus pneumoniae== | | ==Crystal structure of MCAT from Streptococcus pneumoniae== |
| - | <StructureSection load='3im8' size='340' side='right' caption='[[3im8]], [[Resolution|resolution]] 2.10Å' scene=''> | + | <StructureSection load='3im8' size='340' side='right'caption='[[3im8]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3im8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strr6 Strr6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IM8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3IM8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3im8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_pneumoniae_R6 Streptococcus pneumoniae R6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IM8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IM8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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]] 2.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3im9|3im9]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=171101 STRR6])</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=3im8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3im8 OCA], [https://pdbe.org/3im8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3im8 RCSB], [https://www.ebi.ac.uk/pdbsum/3im8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3im8 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Acyl-carrier-protein]_S-malonyltransferase [Acyl-carrier-protein] S-malonyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.39 2.3.1.39] </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=3im8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3im8 OCA], [http://pdbe.org/3im8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3im8 RCSB], [http://www.ebi.ac.uk/pdbsum/3im8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3im8 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8DR16_STRR6 Q8DR16_STRR6] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strr6]] | + | [[Category: Large Structures]] |
| - | [[Category: Hong, S K]] | + | [[Category: Streptococcus pneumoniae R6]] |
| - | [[Category: Kim, E E]] | + | [[Category: Hong SK]] |
| - | [[Category: Kim, K H]] | + | [[Category: Kim EE]] |
| - | [[Category: Kim, Y M]] | + | [[Category: Kim KH]] |
| - | [[Category: Park, J K]] | + | [[Category: Kim YM]] |
| - | [[Category: Acyltransferase]] | + | [[Category: Park JK]] |
| - | [[Category: Fabd]]
| + | |
| - | [[Category: Fatty acid synthesis]]
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| - | [[Category: Malonyl-coa]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
Q8DR16_STRR6
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
Malonyl-CoA-acyl carrier protein transacylase (MCAT) transfers the malonyl group from malonyl-CoA to holo-acyl carrier protein (ACP), and since malonyl-ACP is a key building block for fatty-acid biosynthesis it is considered as a promising antibacterial target. The crystal structures of MCAT from Staphylococcus aureus and Streptococcus pneumoniae have been determined at 1.46 and 2.1A resolution, respectively. In the SaMCAT structure, the N-terminal expression peptide of a neighboring molecule running in the opposite direction of malonyl-CoA makes extensive interactions with the highly conserved "Gly-Gln-Gly-Ser-Gln" stretch, suggesting a new design platform. Mutagenesis results suggest that Ser91 and His199 are the catalytic dyad.
New design platform for malonyl-CoA-acyl carrier protein transacylase.,Hong SK, Kim KH, Park JK, Jeong KW, Kim Y, Kim EE FEBS Lett. 2010 Mar 19;584(6):1240-4. Epub 2010 Feb 19. PMID:20176020[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Hong SK, Kim KH, Park JK, Jeong KW, Kim Y, Kim EE. New design platform for malonyl-CoA-acyl carrier protein transacylase. FEBS Lett. 2010 Mar 19;584(6):1240-4. Epub 2010 Feb 19. PMID:20176020 doi:10.1016/j.febslet.2010.02.038
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