5gm2

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<StructureSection load='5gm2' size='340' side='right'caption='[[5gm2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='5gm2' size='340' side='right'caption='[[5gm2]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5gm2]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/"streptomyces_blastmyceticus"_watanabe_et_al._1957 "streptomyces blastmyceticus" watanabe et al. 1957]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GM2 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5GM2 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5gm2]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_blastmyceticus Streptomyces blastmyceticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GM2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GM2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=TEX:(2S,5S)-9-[(3R)-3,7-DIMETHYLOCTA-1,6-DIEN-3-YL]-5-(HYDROXYMETHYL)-1-METHYL-2-(PROPAN-2-YL)-1,2,4,5,6,8-HEXAHYDRO-3H-[1,4]DIAZONINO[7,6,5-CD]INDOL-3-ONE'>TEX</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gm1|5gm1]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>, <scene name='pdbligand=TEX:(2S,5S)-9-[(3R)-3,7-DIMETHYLOCTA-1,6-DIEN-3-YL]-5-(HYDROXYMETHYL)-1-METHYL-2-(PROPAN-2-YL)-1,2,4,5,6,8-HEXAHYDRO-3H-[1,4]DIAZONINO[7,6,5-CD]INDOL-3-ONE'>TEX</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tleD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=68180 "Streptomyces blastmyceticus" Watanabe et al. 1957])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gm2 OCA], [https://pdbe.org/5gm2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gm2 RCSB], [https://www.ebi.ac.uk/pdbsum/5gm2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gm2 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5gm2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gm2 OCA], [http://pdbe.org/5gm2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gm2 RCSB], [http://www.ebi.ac.uk/pdbsum/5gm2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gm2 ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A0A077K7L1_9ACTN A0A077K7L1_9ACTN]
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TleD is an S-adenosyl-L-methionine dependent methyltransferase and acts as one of the key enzymes in the teleocidin B biosynthesis pathway. Besides the methyl transferring, TleD also rearranges the geranyl and indole moiety of the precursor to form a six-membered ring. Moreover, it does not show homologies to any known terpenoid cyclases. In order to elucidate how such a remarkable reaction could be achieved, we determined the complex crystal structures of TleD and the cofactor analogue S-adenosyl-L-homocysteine with or without substrate teleocidin A1. A domain-swapped pattern via an additional N-terminal alpha-helix is observed in TleD hexamers. The structural comparison and alignment shows this additional N-terminal alpha-helix is the common feature of SAM-MTase-like cyclases TleD and SpnF. The residue Tyr21 anchors the additional N-terminal alpha-helix to "core SAM-MT fold" and is a key residue for catalytical activity. Molecular dynamic simulation results suggest that the dihedral angle C23-C24-C25-C26 of teleocidin A1 is preferred to 60 degrees - 90 degrees in the TleD and substrate complex structure, which tend to adopt a Re-face stereocenter at C25 position after reaction and is according to in vitro enzyme reaction experiments. Our results also demonstrate methyl transfer can be a new chemical strategy for carbocation formation in the terpene cyclization, which is the key initial step.
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Crystal Structure and Enantioselectivity of Terpene Cyclization in SAM Dependent Methyltransferase TleD.,Yu F, Li M, Xu C, Sun B, Zhou H, Wang Z, Xu Q, Xie M, Zuo G, Huang P, Guo H, Wang Q, He J Biochem J. 2016 Sep 9. pii: BCJ20160695. PMID:27613858<ref>PMID:27613858</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5gm2" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
*[[SAM-dependent methyltrasferase 3D structures|SAM-dependent methyltrasferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Streptomyces blastmyceticus watanabe et al. 1957]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: He, J H]]
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[[Category: Streptomyces blastmyceticus]]
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[[Category: Huang, P]]
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[[Category: He JH]]
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[[Category: Li, M J]]
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[[Category: Huang P]]
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[[Category: Sun, B]]
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[[Category: Li MJ]]
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[[Category: Wang, Q S]]
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[[Category: Sun B]]
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[[Category: Wang, Z J]]
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[[Category: Wang QS]]
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[[Category: Xie, M Y]]
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[[Category: Wang ZJ]]
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[[Category: Xu, C Y]]
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[[Category: Xie MY]]
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[[Category: Xu, Q]]
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[[Category: Xu CY]]
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[[Category: Yu, F]]
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[[Category: Xu Q]]
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[[Category: Zhou, H]]
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[[Category: Yu F]]
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[[Category: Zuo, G]]
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[[Category: Zhou H]]
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[[Category: Methyltransferase]]
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[[Category: Zuo G]]
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[[Category: Teleocidin]]
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[[Category: Terpene cyclization]]
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[[Category: Tled]]
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[[Category: Transferase]]
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Current revision

Crystal structure of methyltransferase TleD complexed with SAH and teleocidin A1

PDB ID 5gm2

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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