|
|
| (One intermediate revision not shown.) |
| Line 3: |
Line 3: |
| | <StructureSection load='1gxn' size='340' side='right'caption='[[1gxn]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1gxn' size='340' side='right'caption='[[1gxn]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1gxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"cellvibrio_cellulosa"_nagy_et_al._2002 "cellvibrio cellulosa" nagy et al. 2002]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1gxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Cellvibrio_japonicus Cellvibrio japonicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXN FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gxm|1gxm]], [[1gxo|1gxo]]</div></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]] 1.5Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pectate_lyase Pectate lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.2.2 4.2.2.2] </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=1gxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxn OCA], [https://pdbe.org/1gxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxn RCSB], [https://www.ebi.ac.uk/pdbsum/1gxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxn 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=1gxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxn OCA], [https://pdbe.org/1gxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxn RCSB], [https://www.ebi.ac.uk/pdbsum/1gxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxn ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9F7L3_CELJA Q9F7L3_CELJA] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 31: |
Line 32: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Cellvibrio cellulosa nagy et al. 2002]] | + | [[Category: Cellvibrio japonicus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pectate lyase]]
| + | [[Category: Black GW]] |
| - | [[Category: Black, G W]] | + | [[Category: Brown IE]] |
| - | [[Category: Brown, I E]] | + | [[Category: Charnock SJ]] |
| - | [[Category: Charnock, S J]] | + | [[Category: Davies GJ]] |
| - | [[Category: Davies, G J]] | + | [[Category: Turkenburg JP]] |
| - | [[Category: Turkenburg, J P]] | + | |
| - | [[Category: Elimination]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: Pectate]]
| + | |
| Structural highlights
Function
Q9F7L3_CELJA
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
Enzyme-catalyzed beta-elimination of sugar uronic acids, exemplified by the degradation of plant cell wall pectins, plays an important role in a wide spectrum of biological processes ranging from the recycling of plant biomass through to pathogen virulence. The three-dimensional crystal structure of the catalytic module of a "family PL-10" polysaccharide lyase, Pel10Acm from Cellvibrio japonicus, solved at a resolution of 1.3 A, reveals a new polysaccharide lyase fold and is the first example of a polygalacturonic acid lyase that does not exhibit the "parallel beta-helix" topology. The "Michaelis" complex of an inactive mutant in association with the substrate trigalacturonate/Ca2+ reveals the catalytic machinery harnessed by this polygalacturonate lyase, which displays a stunning resemblance, presumably through convergent evolution, to the tetragalacturonic acid complex observed for a structurally unrelated polygalacturonate lyase from family PL-1. Common coordination of the -1 and +1 subsite saccharide carboxylate groups by a protein-liganded Ca2+ ion, the positioning of an arginine catalytic base in close proximity to the alpha-carbon hydrogen and numerous other conserved enzyme-substrate interactions, considered in light of mutagenesis data for both families, suggest a generic polysaccharide anti-beta-elimination mechanism.
Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases.,Charnock SJ, Brown IE, Turkenburg JP, Black GW, Davies GJ Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12067-72. Epub 2002 Sep 9. PMID:12221284[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Charnock SJ, Brown IE, Turkenburg JP, Black GW, Davies GJ. Convergent evolution sheds light on the anti-beta -elimination mechanism common to family 1 and 10 polysaccharide lyases. Proc Natl Acad Sci U S A. 2002 Sep 17;99(19):12067-72. Epub 2002 Sep 9. PMID:12221284 doi:10.1073/pnas.182431199
|
