3wjn: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 3wjn is ~~ON HOLD~~

==Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)==

== Structural highlights ==

<table><tr><td colspan='2'>[[3wjn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O104:H4_str._2009EL-2071 Escherichia coli O104:H4 str. 2009EL-2071]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WJN FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPS:S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]+TRIHYDROGEN+THIODIPHOSPHATE'>FPS</scene></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=3wjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjn OCA], [https://pdbe.org/3wjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wjn RCSB], [https://www.ebi.ac.uk/pdbsum/3wjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wjn ProSAT]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone. OPPs belongs to the trans-prenyltransferase class of proteins. The structures of OPPs from Escherichia coli were solved in the apo-form as well as in complexes with IPP and a FPP thio-analog, FsPP, at resolutions of 2.2 to 2.6 A, and revealed the detailed interactions between the ligands and enzyme. At the bottom of the active-site tunnel, M123 and M135 act in concert to form a wall which determines the final chain length. These results represent the first ligand-bound crystal structures of a long-chain trans-prenyltransferase and provide new information on the mechanisms of catalysis and product chain elongation. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.

~~Authors:~~ Han, X. , Chen~~, C. C.~~ , Kuo~~, C. J.~~ , Huang~~, C. H~~ , Zheng Y. , Ko~~, T. P~~ , Zhu, Z. , Feng, X., Oldfield, E, Liang, P.H. ~~, Guo, R~~.T.~~, Ma, Y, H~~.

Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from escherichia coli reveal the catalytic and chain-length determining mechanisms.,Han X, Chen CC, Kuo CJ, Huang CH, Zheng Y, Ko TP, Zhu Z, Feng X, Wang K, Oldfield E, Wang AH, Liang PH, Guo RT, Ma Y Proteins. 2014 Jun 4. doi: 10.1002/prot.24618. PMID:24895191<ref>PMID:24895191</ref>

~~Description~~: ~~Crystal structure of Octaprenyl Pyrophosphate synthase from~~ Escherichia coli ~~with farnesyl S~~-~~thiol-pyrophosphate (FSPP)~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Escherichia coli O104:H4 str. 2009EL-2071]]

[[Category: Large Structures]]

[[Category: Chen CC]]

[[Category: Feng X]]

[[Category: Guo RT]]

[[Category: Han X]]

[[Category: Huang CH]]

[[Category: Ko TP]]

[[Category: Kuo CJ]]

[[Category: Liang PH]]

[[Category: Ma YH]]

[[Category: Oldfield E]]

[[Category: Zheng Y]]

[[Category: Zhu Z]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 3wjn is ON HOLD
+==Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)==
+<StructureSection load='3wjn' size='340' side='right'caption='[[3wjn]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3wjn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O104:H4_str._2009EL-2071 Escherichia coli O104:H4 str. 2009EL-2071]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WJN FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FPS:S-[(2E,6E)-3,7,11-TRIMETHYLDODECA-2,6,10-TRIENYL]+TRIHYDROGEN+THIODIPHOSPHATE'>FPS</scene></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=3wjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wjn OCA], [https://pdbe.org/3wjn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wjn RCSB], [https://www.ebi.ac.uk/pdbsum/3wjn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wjn ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Octaprenyl pyrophosphate synthase (OPPs) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone. OPPs belongs to the trans-prenyltransferase class of proteins. The structures of OPPs from Escherichia coli were solved in the apo-form as well as in complexes with IPP and a FPP thio-analog, FsPP, at resolutions of 2.2 to 2.6 A, and revealed the detailed interactions between the ligands and enzyme. At the bottom of the active-site tunnel, M123 and M135 act in concert to form a wall which determines the final chain length. These results represent the first ligand-bound crystal structures of a long-chain trans-prenyltransferase and provide new information on the mechanisms of catalysis and product chain elongation. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
-Authors: Han, X. , Chen, C. C. , Kuo, C. J. , Huang, C. H , Zheng Y. , Ko, T. P , Zhu, Z. , Feng, X., Oldfield, E, Liang, P.H. , Guo, R.T., Ma, Y, H.
+Crystal structures of ligand-bound octaprenyl pyrophosphate synthase from escherichia coli reveal the catalytic and chain-length determining mechanisms.,Han X, Chen CC, Kuo CJ, Huang CH, Zheng Y, Ko TP, Zhu Z, Feng X, Wang K, Oldfield E, Wang AH, Liang PH, Guo RT, Ma Y Proteins. 2014 Jun 4. doi: 10.1002/prot.24618. PMID:24895191<ref>PMID:24895191</ref>
-Description: Crystal structure of Octaprenyl Pyrophosphate synthase from Escherichia coli with farnesyl S-thiol-pyrophosphate (FSPP)
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3wjn" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli O104:H4 str. 2009EL-2071]]
+[[Category: Large Structures]]
+[[Category: Chen CC]]
+[[Category: Feng X]]
+[[Category: Guo RT]]
+[[Category: Han X]]
+[[Category: Huang CH]]
+[[Category: Ko TP]]
+[[Category: Kuo CJ]]
+[[Category: Liang PH]]
+[[Category: Ma YH]]
+[[Category: Oldfield E]]
+[[Category: Zheng Y]]
+[[Category: Zhu Z]]