4dqn
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==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 [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='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='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> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/Q8DTW7_STRMU Q8DTW7_STRMU] | ||
+ | <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> | ||
+ | <div class="pdbe-citations 4dqn" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Streptococcus mutans]] | ||
+ | [[Category: Li ST]] | ||
+ | [[Category: Ruan J]] |
Current revision
Crystal structure of the branched-chain aminotransferase from Streptococcus mutans
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