5gww
From Proteopedia
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==Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue== | ==Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue== | ||
| - | <StructureSection load='5gww' size='340' side='right' caption='[[5gww]], [[Resolution|resolution]] 2.30Å' scene=''> | + | <StructureSection load='5gww' size='340' side='right'caption='[[5gww]], [[Resolution|resolution]] 2.30Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5gww]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[5gww]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14672_[[streptomyces_ghanaensis]] Atcc 14672 [[streptomyces ghanaensis]]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GWW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GWW FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7B5:methyl+(2R)-3-dimethoxyphosphoryloxy-2-[(2Z,6E)-3,7,11-trimethyldodeca-2,6,10-trienoxy]propanoate'>7B5</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=7B5:methyl+(2R)-3-dimethoxyphosphoryloxy-2-[(2Z,6E)-3,7,11-trimethyldodeca-2,6,10-trienoxy]propanoate'>7B5</scene></td></tr> | ||
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b02|5b02]], [[5gwv|5gwv]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5b02|5b02]], [[5gwv|5gwv]], [[6j8w|6j8w]], [[6j8v|6j8v]]</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sso7d, sso7d-1, SSO10610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sso7d, sso7d-1, SSO10610 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67581 ATCC 14672 [[Streptomyces ghanaensis]]])</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=5gww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gww OCA], [http://pdbe.org/5gww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gww RCSB], [http://www.ebi.ac.uk/pdbsum/5gww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gww ProSAT]</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=5gww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gww OCA], [http://pdbe.org/5gww PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gww RCSB], [http://www.ebi.ac.uk/pdbsum/5gww PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gww ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The antibiotic moenomycin A is a phosphoglycerate derivative with a C25-moenocinyl chain and a branched oligosaccharide. Formation of the C25-chain is catalyzed by the enzyme MoeN5 with geranyl pyrophosphate (GPP) and the sugar-linked 2-Z,E-farnesyl-3-phosphoglycerate (FPG) as its substrates. Previous complex crystal structures with GPP and long-chain alkyl glycosides suggested that GPP binds to the S1 site in a similar way as in most other alpha-helical prenyltransferases (PTs), and FPG is likely to assume a bent conformation in the S2 site. However, two FPG derivatives synthesized in the current study were found in the S1 site rather than S2 in their complex crystal structures with MoeN5. Apparently S1 is the preferred site for prenyl-containing ligand, and S2 binding may proceed only after S1 is occupied. Thus, like most trans-type PTs, MoeN5 may employ a sequential ionization-condensation-elimination mechanism that involves a carbocation intermediate. | ||
| + | |||
| + | Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism.,Zhang L, Ko TP, Malwal SR, Liu W, Zhou S, Yu X, Oldfield E, Guo RT, Chen CC Biochem Biophys Res Commun. 2019 Apr 16;511(4):800-805. doi:, 10.1016/j.bbrc.2019.02.131. Epub 2019 Mar 2. PMID:30837154<ref>PMID:30837154</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5gww" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
[[Category: Chen, C C]] | [[Category: Chen, C C]] | ||
[[Category: Guo, R T]] | [[Category: Guo, R T]] | ||
Revision as of 07:56, 3 April 2019
Structure of MoeN5-Sso7d fusion protein in complex with a permethylated substrate analogue
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