|
|
| Line 3: |
Line 3: |
| | <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/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> | + | <table><tr><td colspan='2'>[[5gww]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2] and [https://en.wikipedia.org/wiki/Streptomyces_viridosporus Streptomyces viridosporus]. 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 [https://proteopedia.org/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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='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'>[https://proteopedia.org/fgij/fg.htm?mol=5gww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gww OCA], [https://pdbe.org/5gww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gww RCSB], [https://www.ebi.ac.uk/pdbsum/5gww PDBsum], [https://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> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/A0A010_STRVD A0A010_STRVD] [https://www.uniprot.org/uniprot/DN7D_SACS2 DN7D_SACS2] Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Stimulates the Holliday junction cleavage activity of Hjc (PubMed:11709558).[UniProtKB:P61990]<ref>PMID:11709558</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 23: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chen, C C]] | + | [[Category: Saccharolobus solfataricus P2]] |
| - | [[Category: Guo, R T]] | + | [[Category: Streptomyces viridosporus]] |
| - | [[Category: Ko, T P]] | + | [[Category: Chen C-C]] |
| - | [[Category: Alpha helical]] | + | [[Category: Guo R-T]] |
| - | [[Category: Antibiotic]] | + | [[Category: Ko T-P]] |
| - | [[Category: Biosynthesis]]
| + | |
| - | [[Category: Dna binding protein]]
| + | |
| - | [[Category: Moenomycin]]
| + | |
| - | [[Category: Prenyl transferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
A0A010_STRVD DN7D_SACS2 Can constrain negative DNA supercoils. May be involved in maintaining the integrity of the genome at high temperature (By similarity). Stimulates the Holliday junction cleavage activity of Hjc (PubMed:11709558).[UniProtKB:P61990][1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kvaratskhelia M, Wardleworth BN, Bond CS, Fogg JM, Lilley DM, White MF. Holliday junction resolution is modulated by archaeal chromatin components in vitro. J Biol Chem. 2002 Jan 25;277(4):2992-6. Epub 2001 Nov 14. PMID:11709558 doi:http://dx.doi.org/10.1074/jbc.M109496200
- ↑ Zhang L, Ko TP, Malwal SR, Liu W, Zhou S, Yu X, Oldfield E, Guo RT, Chen CC. Complex structures of MoeN5 with substrate analogues suggest sequential catalytic mechanism. 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 doi:http://dx.doi.org/10.1016/j.bbrc.2019.02.131
|
