|
|
| Line 3: |
Line 3: |
| | <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 [http://en.wikipedia.org/wiki/American_tobacco American tobacco]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1QGN FirstGlance]. <br> | + | <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='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> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">METB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4097 American tobacco])</td></tr> | + | <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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cystathionine_gamma-synthase Cystathionine gamma-synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.48 2.5.1.48] </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=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'>[http://proteopedia.org/fgij/fg.htm?mol=1qgn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgn OCA], [http://pdbe.org/1qgn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qgn RCSB], [http://www.ebi.ac.uk/pdbsum/1qgn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qgn ProSAT]</span></td></tr> | + | |
| | </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]] |
| Line 30: |
Line 31: |
| | | | |
| | ==See Also== | | ==See Also== |
| | + | *[[Cystathionine beta-lyase|Cystathionine beta-lyase]] |
| | *[[Cystathionine gamma synthase|Cystathionine gamma synthase]] | | *[[Cystathionine gamma synthase|Cystathionine gamma synthase]] |
| | == References == | | == References == |
| Line 35: |
Line 37: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: American tobacco]] | |
| - | [[Category: Cystathionine gamma-synthase]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Clausen, T]] | + | [[Category: Nicotiana tabacum]] |
| - | [[Category: Huber, R]] | + | [[Category: Clausen T]] |
| - | [[Category: Laber, B]] | + | [[Category: Huber R]] |
| - | [[Category: Messerschmidt, A]] | + | [[Category: Laber B]] |
| - | [[Category: Steegborn, C]] | + | [[Category: Messerschmidt A]] |
| - | [[Category: Streber, W]] | + | [[Category: Steegborn C]] |
| - | [[Category: Gamma-family]]
| + | [[Category: Streber W]] |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Methionine biosynthesis]]
| + | |
| - | [[Category: Pyridoxal 5'-phosphate]]
| + | |
| Structural highlights
Function
Q9ZPL5_TOBAC
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
Cystathionine 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 Also
References
- ↑ Steegborn C, Messerschmidt A, Laber B, Streber W, Huber R, Clausen T. The crystal structure of cystathionine gamma-synthase from Nicotiana tabacum reveals its substrate and reaction specificity. J Mol Biol. 1999 Jul 30;290(5):983-96. PMID:10438597 doi:10.1006/jmbi.1999.2935
|
