3p16: Difference between revisions
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[[ | ==Crystal structure of DNA polymerase III sliding clamp== | ||
<StructureSection load='3p16' size='340' side='right' caption='[[3p16]], [[Resolution|resolution]] 2.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3p16]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P16 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3P16 FirstGlance]. <br> | |||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaN, Rv0002, MT0002, MTV029.02, MTCY10H4.0 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </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=3p16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p16 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3p16 RCSB], [http://www.ebi.ac.uk/pdbsum/3p16 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The sliding clamp is a key component of DNA polymerase III (Pol III) required for genome replication. It is known to function with diverse DNA repair proteins and cell cycle-control proteins, making it a potential drug target. To extend our understanding of the structure/function relationship of the sliding clamp, we solved the crystal structure of the sliding clamp from Mycobacterium tuberculosis (M. tuberculosis), a human pathogen that causes most cases of tuberculosis (TB). The sliding clamp from M. tuberculosis forms a ring-shaped head-to-tail dimer with three domains per subunit. Each domain contains two alpha helices in the inner ring that lie against two beta sheets in the outer ring. Previous studies have indicated that many Escherichia coli clamp-binding proteins have a conserved LF sequence, which is critical for binding to the hydrophobic region of the sliding clamp. Here, we analyzed the binding affinities of the M. tuberculosis sliding clamp and peptides derived from the alpha and delta subunits of Pol III, which indicated that the LF motif also plays an important role in the binding of the alpha and delta subunits to the sliding clamp of M. tuberculosis. | |||
Crystal structure of DNA polymerase III beta sliding clamp from Mycobacterium tuberculosis.,Gui WJ, Lin SQ, Chen YY, Zhang XE, Bi LJ, Jiang T Biochem Biophys Res Commun. 2011 Feb 11;405(2):272-7. Epub 2011 Jan 8. PMID:21219854<ref>PMID:21219854</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[DNA polymerase|DNA polymerase]] | *[[DNA polymerase|DNA polymerase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: DNA-directed DNA polymerase]] | [[Category: DNA-directed DNA polymerase]] | ||
[[Category: Mycobacterium tuberculosis]] | [[Category: Mycobacterium tuberculosis]] | ||
[[Category: Bi, L J | [[Category: Bi, L J]] | ||
[[Category: Chen, Y Y | [[Category: Chen, Y Y]] | ||
[[Category: Gui, W J | [[Category: Gui, W J]] | ||
[[Category: Jiang, T | [[Category: Jiang, T]] | ||
[[Category: Lin, S Q | [[Category: Lin, S Q]] | ||
[[Category: Zhang, X E | [[Category: Zhang, X E]] | ||
[[Category: Dna polymerase iii sliding clamp]] | [[Category: Dna polymerase iii sliding clamp]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 14:34, 9 December 2014
Crystal structure of DNA polymerase III sliding clampCrystal structure of DNA polymerase III sliding clamp
Structural highlights
Publication Abstract from PubMedThe sliding clamp is a key component of DNA polymerase III (Pol III) required for genome replication. It is known to function with diverse DNA repair proteins and cell cycle-control proteins, making it a potential drug target. To extend our understanding of the structure/function relationship of the sliding clamp, we solved the crystal structure of the sliding clamp from Mycobacterium tuberculosis (M. tuberculosis), a human pathogen that causes most cases of tuberculosis (TB). The sliding clamp from M. tuberculosis forms a ring-shaped head-to-tail dimer with three domains per subunit. Each domain contains two alpha helices in the inner ring that lie against two beta sheets in the outer ring. Previous studies have indicated that many Escherichia coli clamp-binding proteins have a conserved LF sequence, which is critical for binding to the hydrophobic region of the sliding clamp. Here, we analyzed the binding affinities of the M. tuberculosis sliding clamp and peptides derived from the alpha and delta subunits of Pol III, which indicated that the LF motif also plays an important role in the binding of the alpha and delta subunits to the sliding clamp of M. tuberculosis. Crystal structure of DNA polymerase III beta sliding clamp from Mycobacterium tuberculosis.,Gui WJ, Lin SQ, Chen YY, Zhang XE, Bi LJ, Jiang T Biochem Biophys Res Commun. 2011 Feb 11;405(2):272-7. Epub 2011 Jan 8. PMID:21219854[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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