1qgn: Difference between revisions
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<StructureSection load='1qgn' size='340' side='right'caption='[[1qgn]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1qgn' size='340' side='right'caption='[[1qgn]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qgn]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1qgn]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Nicotiana_tabacum Nicotiana tabacum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QGN FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1qgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgn OCA], [https://pdbe.org/1qgn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qgn RCSB], [https://www.ebi.ac.uk/pdbsum/1qgn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qgn ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9ZPL5_TOBAC Q9ZPL5_TOBAC] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Cystathionine beta-lyase|Cystathionine beta-lyase]] | |||
*[[Cystathionine gamma synthase|Cystathionine gamma synthase]] | *[[Cystathionine gamma synthase|Cystathionine gamma synthase]] | ||
== References == | == References == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Clausen | [[Category: Nicotiana tabacum]] | ||
[[Category: Huber | [[Category: Clausen T]] | ||
[[Category: Laber | [[Category: Huber R]] | ||
[[Category: Messerschmidt | [[Category: Laber B]] | ||
[[Category: Steegborn | [[Category: Messerschmidt A]] | ||
[[Category: Streber | [[Category: Steegborn C]] | ||
[[Category: Streber W]] | |||
Latest revision as of 13:02, 16 August 2023
CYSTATHIONINE GAMMA-SYNTHASE FROM NICOTIANA TABACUMCYSTATHIONINE GAMMA-SYNTHASE FROM NICOTIANA TABACUM
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCystathionine gamma-synthase catalyses the committed step of de novo methionine biosynthesis in micro-organisms and plants, making the enzyme an attractive target for the design of new antibiotics and herbicides. The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum has been solved by Patterson search techniques using the structure of Escherichia coli cystathionine gamma-synthase. The model was refined at 2.9 A resolution to a crystallographic R -factor of 20.1 % (Rfree25.0 %). The physiological substrates of the enzyme, L-homoserine phosphate and L-cysteine, were modelled into the unliganded structure. These complexes support the proposed ping-pong mechanism for catalysis and illustrate the dissimilar substrate specificities of bacterial and plant cystathionine gamma-synthases on a molecular level. The main difference arises from the binding modes of the distal substrate groups (O -acetyl/succinyl versusO -phosphate). Central in fixing the distal phosphate of the plant CGS substrate is an exposed lysine residue that is strictly conserved in plant cystathionine gamma-synthases whereas bacterial enzymes carry a glycine residue at this position. General insight regarding the reaction specificity of transsulphuration enzymes is gained by the comparison to cystathionine beta-lyase from E. coli, indicating the mechanistic importance of a second substrate binding site for L-cysteine which leads to different chemical reaction types. The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity.,Steegborn C, Messerschmidt A, Laber B, Streber W, Huber R, Clausen T J Mol Biol. 1999 Jul 30;290(5):983-96. PMID:10438597[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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