3vx4: Difference between revisions
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The | ==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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3VX4 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]] 2.69Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=3vx4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vx4 OCA], [https://pdbe.org/3vx4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vx4 RCSB], [https://www.ebi.ac.uk/pdbsum/3vx4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vx4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8DW05_STRMU Q8DW05_STRMU] | |||
<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> | |||
<div class="pdbe-citations 3vx4" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Streptococcus mutans UA159]] | |||
[[Category: Hayashi H]] | |||
[[Category: Ishii S]] | |||
[[Category: Murakawa T]] | |||
[[Category: Okamoto A]] | |||
[[Category: Yano T]] | |||
