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| | <StructureSection load='4lvc' size='340' side='right'caption='[[4lvc]], [[Resolution|resolution]] 1.74Å' scene=''> | | <StructureSection load='4lvc' size='340' side='right'caption='[[4lvc]], [[Resolution|resolution]] 1.74Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4lvc]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_49852 Atcc 49852]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LVC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4lvc]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bradyrhizobium_elkanii Bradyrhizobium elkanii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LVC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LVC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</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]] 1.74Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ond|3ond]], [[3one|3one]], [[3onf|3onf]], [[1li4|1li4]], [[1b3r|1b3r]], [[3n58|3n58]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BeSAHase ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29448 ATCC 49852])</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=4lvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvc OCA], [https://pdbe.org/4lvc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lvc RCSB], [https://www.ebi.ac.uk/pdbsum/4lvc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvc ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=4lvc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lvc OCA], [http://pdbe.org/4lvc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lvc RCSB], [http://www.ebi.ac.uk/pdbsum/4lvc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lvc ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/SAHH_BRAEL SAHH_BRAEL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Adenosylhomocysteinase]] | + | [[Category: Bradyrhizobium elkanii]] |
| - | [[Category: Atcc 49852]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Imiolczyk, B]] | + | [[Category: Imiolczyk B]] |
| - | [[Category: Jaskolski, M]] | + | [[Category: Jaskolski M]] |
| - | [[Category: Manszewski, T]] | + | [[Category: Manszewski T]] |
| - | [[Category: Singh, K]] | + | [[Category: Singh K]] |
| - | [[Category: Atmospheric nitrogen fixation]]
| + | |
| - | [[Category: Cellular methylation]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Nad+ cofactor]]
| + | |
| - | [[Category: Nad+ cofactor complex]]
| + | |
| - | [[Category: Rhizobium-legume symbiosis]]
| + | |
| - | [[Category: Sah hydrolysis]]
| + | |
| Structural highlights
4lvc is a 4 chain structure with sequence from Bradyrhizobium elkanii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Method: | X-ray diffraction, Resolution 1.74Å |
| Ligands: | , , , , |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
SAHH_BRAEL
Publication Abstract from PubMed
S-Adenosyl-L-homocysteine hydrolase (SAHase) is involved in the enzymatic regulation of S-adenosyl-L-methionine (SAM)-dependent methylation reactions. After methyl-group transfer from SAM, S-adenosyl-L-homocysteine (SAH) is formed as a byproduct, which in turn is hydrolyzed to adenosine (Ado) and homocysteine (Hcy) by SAHase. The crystal structure of BeSAHase, an SAHase from Bradyrhizobium elkanii, which is a nitrogen-fixing bacterial symbiont of legume plants, was determined at 1.7 A resolution, showing the domain organization (substrate-binding domain, NAD(+) cofactor-binding domain and dimerization domain) of the subunits. The protein crystallized in its biologically relevant tetrameric form, with three subunits in a closed conformation enforced by complex formation with the Ado product of the enzymatic reaction. The fourth subunit is ligand-free and has an open conformation. The BeSAHase structure therefore provides a unique snapshot of the domain movement of the enzyme induced by the binding of its natural ligands.
An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii.,Manszewski T, Singh K, Imiolczyk B, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2422-32. doi:, 10.1107/S1399004715018659. Epub 2015 Nov 26. PMID:26627650[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Manszewski T, Singh K, Imiolczyk B, Jaskolski M. An enzyme captured in two conformational states: crystal structure of S-adenosyl-L-homocysteine hydrolase from Bradyrhizobium elkanii. Acta Crystallogr D Biol Crystallogr. 2015 Dec 1;71(Pt 12):2422-32. doi:, 10.1107/S1399004715018659. Epub 2015 Nov 26. PMID:26627650 doi:http://dx.doi.org/10.1107/S1399004715018659
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