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| | ==Crystal structure of the branched-chain aminotransferase from Streptococcus mutans== | | ==Crystal structure of the branched-chain aminotransferase from Streptococcus mutans== |
| - | <StructureSection load='4dqn' size='340' side='right' caption='[[4dqn]], [[Resolution|resolution]] 1.97Å' scene=''> | + | <StructureSection load='4dqn' size='340' side='right'caption='[[4dqn]], [[Resolution|resolution]] 1.97Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4dqn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_25175 Atcc 25175]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DQN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DQN FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4dqn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_mutans Streptococcus mutans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DQN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DQN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ilvE, SMU_1203 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1309 ATCC 25175])</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]] 1.97Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Branched-chain-amino-acid_transaminase Branched-chain-amino-acid transaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.6.1.42 2.6.1.42] </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=4dqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqn OCA], [https://pdbe.org/4dqn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dqn RCSB], [https://www.ebi.ac.uk/pdbsum/4dqn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dqn ProSAT]</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=4dqn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dqn OCA], [http://pdbe.org/4dqn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dqn RCSB], [http://www.ebi.ac.uk/pdbsum/4dqn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dqn ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8DTW7_STRMU Q8DTW7_STRMU] |
| | <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: Atcc 25175]] | + | [[Category: Large Structures]] |
| - | [[Category: Branched-chain-amino-acid transaminase]] | + | [[Category: Streptococcus mutans]] |
| - | [[Category: Li, S T]] | + | [[Category: Li ST]] |
| - | [[Category: Ruan, J]] | + | [[Category: Ruan J]] |
| - | [[Category: Aminotransferase]]
| + | |
| - | [[Category: Transferase]]
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| Structural highlights
Function
Q8DTW7_STRMU
Publication Abstract from PubMed
The branched-chain amino-acid aminotransferase from Streptococcus mutans (SmIlvE) was recombinantly expressed in Escherichia coli with high yield. An effective purification protocol was established. A bioactivity assay indicated that SmIlvE had aminotransferase activity. The specific activity of SmIlvE towards amino-acid substrates was found to be as follows (in descending order): Ile > Leu > Val > Trp > Gly. The protein was crystallized using the hanging-drop vapour-diffusion method with PEG 3350 as the primary precipitant. The structure of SmIlvE was solved at 1.97 A resolution by the molecular-replacement method. Comparison with structures of homologous proteins enabled the identification of conserved structural elements that might play a role in substrate binding. Further work is needed to confirm the interaction between SmIlvE and its substrates by determining the structures of their complexes.
Structure of the branched-chain aminotransferase from Streptococcus mutans.,Ruan J, Hu J, Yin A, Wu W, Cong X, Feng X, Li S Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):996-1002. Epub 2012 Jul, 17. PMID:22868765[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ruan J, Hu J, Yin A, Wu W, Cong X, Feng X, Li S. Structure of the branched-chain aminotransferase from Streptococcus mutans. Acta Crystallogr D Biol Crystallogr. 2012 Aug;68(Pt 8):996-1002. Epub 2012 Jul, 17. PMID:22868765 doi:http://dx.doi.org/10.1107/S0907444912018446
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