4dqn
From Proteopedia
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| - | [[ | + | ==Crystal structure of the branched-chain aminotransferase from Streptococcus mutans== |
| + | <StructureSection load='4dqn' size='340' side='right' caption='[[4dqn]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4dqn]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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 Streptococcus mutans])</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'>[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://www.rcsb.org/pdb/explore.do?structureId=4dqn RCSB], [http://www.ebi.ac.uk/pdbsum/4dqn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:22868765</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Branched-chain-amino-acid transaminase]] | [[Category: Branched-chain-amino-acid transaminase]] | ||
[[Category: Streptococcus mutans]] | [[Category: Streptococcus mutans]] | ||
| - | [[Category: Li, S T | + | [[Category: Li, S T]] |
| - | [[Category: Ruan, J | + | [[Category: Ruan, J]] |
[[Category: Aminotransferase]] | [[Category: Aminotransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 16:55, 9 December 2014
Crystal structure of the branched-chain aminotransferase from Streptococcus mutans
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