3vx4: Difference between revisions
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==Crystal Structure of the Nucleotide-Binding Domain of S. mutans ComA, a Bifunctional ATP-binding Cassette Transporter Involved in the Quorum-sensing Pathway== | |||
<StructureSection load='3vx4' size='340' side='right' caption='[[3vx4]], [[Resolution|resolution]] 2.69Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3vx4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptococcus_mutans_ua159 Streptococcus mutans ua159]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VX4 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMU_286 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210007 Streptococcus mutans UA159])</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=3vx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vx4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vx4 RCSB], [http://www.ebi.ac.uk/pdbsum/3vx4 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The ATP-binding cassette (ABC) transporter ComA is a key molecule essential for the first step of the quorum-sensing system of Streptococcus. The nucleotide binding domains (NBD) of Streptococcus mutans ComA with different N termini, NBD1 (amino acid residues 495-760), NBD2 (517-760), and NBD3 (528-760), were expressed, purified, and characterized. The shortest NBD3 corresponds to the region commonly defined as NBD in the database searches of ABC transporters. A kinetic analysis showed that the extra N-terminal region conferred a significantly higher ATP hydrolytic activity on the NBD at a neutral pH. Gel-filtration, X-ray crystallography, and mutational analyses suggest that at least four to five residues beyond the N-terminal boundary of NBD3 indeed participate in stabilizing the protein scaffold of the domain structure, thereby facilitating the ATP-dependent dimerization of NBD which is a prerequisite to the catalysis. These findings, together with the presence of a highly conserved glycine residue in this region, support the redefinition of the N-terminal boundary of the NBD of these types of ABC exporters. | |||
Boundary of the Nucleotide-Binding Domain of Streptococcus ComA Based on Functional and Structural Analysis.,Ishii S, Yano T, Okamoto A, Murakawa T, Hayashi H Biochemistry. 2013 Apr 16;52(15):2545-55. doi: 10.1021/bi3017069. Epub 2013 Apr, 5. PMID:23534432<ref>PMID:23534432</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Streptococcus mutans ua159]] | [[Category: Streptococcus mutans ua159]] | ||
[[Category: Hayashi, H | [[Category: Hayashi, H]] | ||
[[Category: Ishii, S | [[Category: Ishii, S]] | ||
[[Category: Murakawa, T | [[Category: Murakawa, T]] | ||
[[Category: Okamoto, A | [[Category: Okamoto, A]] | ||
[[Category: Yano, T | [[Category: Yano, T]] | ||
[[Category: Abc transporter]] | [[Category: Abc transporter]] | ||
[[Category: Atp binding]] | [[Category: Atp binding]] | ||
[[Category: Transport protein]] | [[Category: Transport protein]] | ||
