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1g1b

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Revision as of 11:18, 28 July 2021

CHORISMATE LYASE (WILD-TYPE) WITH BOUND PRODUCT

Structural highlights

1g1b is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1fw9
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[UBIC_ECOLI] Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.[HAMAP-Rule:MF_01632]

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

The enzyme chorismate lyase (CL) catalyzes the removal of pyruvate from chorismate to produce 4-hydroxy benzoate (4HB) for the ubiquinone pathway. In Escherichia coli, CL is monomeric, with 164 residues. We have determined the structure of the CL product complex by crystallographic heavy-atom methods and report the structure at 1.4-A resolution for a fully active double Cys-to-Ser mutant and at 2.0-A resolution for the wild-type. The fold involves a 6-stranded antiparallel beta-sheet with no spanning helices and novel connectivity. The product is bound internally, adjacent to the sheet, with its polar groups coordinated by two main-chain amides and by the buried side-chains of Arg 76 and Glu 155. The 4HB is completely sequestered from solvent in a largely hydrophobic environment behind two helix-turn-helix loops. The extensive product binding that is observed is consistent with biochemical measurements of slow product release and 10-fold stronger binding of product than substrate. Substrate binding and kinetically rate-limiting product release apparently require the rearrangement of these active-site-covering loops. Implications for the biological function of the high product binding are considered in light of the unique cellular role of 4HB, which is produced by cytoplasmic CL but is used by the membrane-bound enzyme 4HB octaprenyltransferase.

The crystal structure of chorismate lyase shows a new fold and a tightly retained product.,Gallagher DT, Mayhew M, Holden MJ, Howard A, Kim KJ, Vilker VL Proteins. 2001 Aug 15;44(3):304-11. PMID:11455603^[1]

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

References

↑ Gallagher DT, Mayhew M, Holden MJ, Howard A, Kim KJ, Vilker VL. The crystal structure of chorismate lyase shows a new fold and a tightly retained product. Proteins. 2001 Aug 15;44(3):304-11. PMID:11455603

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g1b"

@@ Line 3: / Line 3: @@
 <StructureSection load='1g1b' size='340' side='right'caption='[[1g1b]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1g1b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1G1B FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1g1b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1B FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHB:P-HYDROXYBENZOIC+ACID'>PHB</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fw9|1fw9]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fw9|1fw9]]</div></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=1g1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1b OCA], [http://pdbe.org/1g1b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1g1b RCSB], [http://www.ebi.ac.uk/pdbsum/1g1b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1b ProSAT]</span></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=1g1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1g1b OCA], [https://pdbe.org/1g1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1g1b RCSB], [https://www.ebi.ac.uk/pdbsum/1g1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1g1b ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UBIC_ECOLI UBIC_ECOLI]] Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.[HAMAP-Rule:MF_01632]
+[[https://www.uniprot.org/uniprot/UBIC_ECOLI UBIC_ECOLI]] Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.[HAMAP-Rule:MF_01632]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1g1b

From Proteopedia

Revision as of 11:18, 28 July 2021

CHORISMATE LYASE (WILD-TYPE) WITH BOUND PRODUCT

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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