View source for 4dqn


==Crystal structure of the branched-chain aminotransferase from Streptococcus mutans==
<StructureSection load='4dqn' size='340' side='right'caption='[[4dqn]], [[Resolution|resolution]] 1.97&Aring;' 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]] 1.97&#8491;</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 &gt; Leu &gt; Val &gt; Trp &gt; 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&reg;/PubMed&reg;, 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]]