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3lgs
From Proteopedia
(Difference between revisions)
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==A. thaliana MTA nucleosidase in complex with S-adenosylhomocysteine== | ==A. thaliana MTA nucleosidase in complex with S-adenosylhomocysteine== | ||
<StructureSection load='3lgs' size='340' side='right' caption='[[3lgs]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='3lgs' size='340' side='right' caption='[[3lgs]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3lgs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3lgs]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LGS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LGS FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jys|1jys]], [[1nc1|1nc1]], [[2qtt|2qtt]], [[2qtg|2qtg]], [[2qsu|2qsu]], [[2h8g|2h8g]], [[1nc3|1nc3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jys|1jys]], [[1nc1|1nc1]], [[2qtt|2qtt]], [[2qtg|2qtg]], [[2qsu|2qsu]], [[2h8g|2h8g]], [[1nc3|1nc3]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT4g38800, atmtan1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT4g38800, atmtan1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> |
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylthioadenosine_nucleosidase Methylthioadenosine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.16 3.2.2.16] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methylthioadenosine_nucleosidase Methylthioadenosine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.16 3.2.2.16] </span></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=3lgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lgs RCSB], [http://www.ebi.ac.uk/pdbsum/3lgs PDBsum]</span></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=3lgs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lgs OCA], [http://pdbe.org/3lgs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lgs RCSB], [http://www.ebi.ac.uk/pdbsum/3lgs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lgs ProSAT]</span></td></tr> |
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MTN1_ARATH MTN1_ARATH]] Enzyme of the methionine cycle that catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Contributes to the maintenance of AdoMet homeostasis and is required to sustain high rates of ethylene synthesis. Inactive towards S-adenosylhomocysteine (SAH/AdoHcy).<ref>PMID:17144895</ref> <ref>PMID:18342331</ref> <ref>PMID:20345605</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lgs ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3lgs" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Arath]] |
[[Category: Methylthioadenosine nucleosidase]] | [[Category: Methylthioadenosine nucleosidase]] | ||
[[Category: Howell, P L]] | [[Category: Howell, P L]] | ||
[[Category: Siu, K K.W]] | [[Category: Siu, K K.W]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
Revision as of 18:49, 4 August 2016
A. thaliana MTA nucleosidase in complex with S-adenosylhomocysteine
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