2gm4: Difference between revisions

Revision as of 18:33, 21 February 2008

An activated, tetrameric gamma-delta resolvase: Hin chimaera bound to cleaved DNA

OverviewOverview

The structures of two mutants of the site-specific recombinase, gammadelta resolvase, that form activated tetramers have been determined. One, at 3.5-A resolution, forms a synaptic intermediate of resolvase that is covalently linked to two cleaved DNAs, whereas the other is of an unliganded structure determined at 2.1-A resolution. Comparisons of the four known tetrameric resolvase structures show that the subunits interact through the formation of a common core of four helices. The N-terminal halves of these helices superimpose well on each other, whereas the orientations of their C termini are more variable. The catalytic domains of resolvase in the unliganded structure are arranged asymmetrically, demonstrating that their positions can move substantially while preserving the four-helix core that forms the tetramer. These results suggest that the precleavage synaptic tetramer of gammadelta resolvase, whose structure is not known, may be formed by a similar four-helix core, but differ in the relative orientations of its catalytic and DNA-binding domains.

About this StructureAbout this Structure

2GM4 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Implications of structures of synaptic tetramers of gamma delta resolvase for the mechanism of recombination., Kamtekar S, Ho RS, Cocco MJ, Li W, Wenwieser SV, Boocock MR, Grindley ND, Steitz TA, Proc Natl Acad Sci U S A. 2006 Jul 11;103(28):10642-7. Epub 2006 Jun 28. PMID:16807292

Page seeded by OCA on Thu Feb 21 17:33:02 2008

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OCA

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-[[Image:2gm4.gif|left|200px]]<br /><applet load="2gm4" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2gm4.gif|left|200px]]<br /><applet load="2gm4" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2gm4, resolution 3.50&Aring;" />
 '''An activated, tetrameric gamma-delta resolvase: Hin chimaera bound to cleaved DNA'''<br />
 ==Overview==
-The structures of two mutants of the site-specific recombinase, gammadelta, resolvase, that form activated tetramers have been determined. One, at, 3.5-A resolution, forms a synaptic intermediate of resolvase that is, covalently linked to two cleaved DNAs, whereas the other is of an, unliganded structure determined at 2.1-A resolution. Comparisons of the, four known tetrameric resolvase structures show that the subunits interact, through the formation of a common core of four helices. The N-terminal, halves of these helices superimpose well on each other, whereas the, orientations of their C termini are more variable. The catalytic domains, of resolvase in the unliganded structure are arranged asymmetrically, demonstrating that their positions can move substantially while preserving, the four-helix core that forms the tetramer. These results suggest that, the precleavage synaptic tetramer of gammadelta resolvase, whose structure, is not known, may be formed by a similar four-helix core, but differ in, the relative orientations of its catalytic and DNA-binding domains.
+The structures of two mutants of the site-specific recombinase, gammadelta resolvase, that form activated tetramers have been determined. One, at 3.5-A resolution, forms a synaptic intermediate of resolvase that is covalently linked to two cleaved DNAs, whereas the other is of an unliganded structure determined at 2.1-A resolution. Comparisons of the four known tetrameric resolvase structures show that the subunits interact through the formation of a common core of four helices. The N-terminal halves of these helices superimpose well on each other, whereas the orientations of their C termini are more variable. The catalytic domains of resolvase in the unliganded structure are arranged asymmetrically, demonstrating that their positions can move substantially while preserving the four-helix core that forms the tetramer. These results suggest that the precleavage synaptic tetramer of gammadelta resolvase, whose structure is not known, may be formed by a similar four-helix core, but differ in the relative orientations of its catalytic and DNA-binding domains.
 ==About this Structure==
-GM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GM4 OCA].
+GM4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GM4 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Ho, R.S.]]
+[[Category: Ho, R S.]]
 [[Category: Kamtekar, S.]]
 [[Category: Li, W.]]
-[[Category: Steitz, T.A.]]
+[[Category: Steitz, T A.]]
 [[Category: gamma delta resolvase]]
 [[Category: protein dna complex]]
 [[Category: site specific recombination]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:16:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:33:02 2008''