1hlv: Difference between revisions

Revision as of 14:02, 21 February 2008

CRYSTAL STRUCTURE OF CENP-B(1-129) COMPLEXED WITH THE CENP-B BOX DNA

OverviewOverview

The human centromere protein B (CENP-B), one of the centromere components, specifically binds a 17 bp sequence (the CENP-B box), which appears in every other alpha-satellite repeat. In the present study, the crystal structure of the complex of the DNA-binding region (129 residues) of CENP-B and the CENP-B box DNA has been determined at 2.5 A resolution. The DNA-binding region forms two helix-turn-helix domains, which are bound to adjacent major grooves of the DNA. The DNA is kinked at the two recognition helix contact sites, and the DNA region between the kinks is straight. Among the major groove protein-bound DNAs, this 'kink-straight-kink' bend contrasts with ordinary 'round bends' (gradual bending between two protein contact sites). The larger kink (43 degrees ) is induced by a novel mechanism, 'phosphate bridging by an arginine-rich helix': the recognition helix with an arginine cluster is inserted perpendicularly into the major groove and bridges the groove through direct interactions with the phosphate groups. The overall bending angle is 59 degrees, which may be important for the centromere-specific chromatin structure.

About this StructureAbout this Structure

1HLV is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the CENP-B protein-DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA., Tanaka Y, Nureki O, Kurumizaka H, Fukai S, Kawaguchi S, Ikuta M, Iwahara J, Okazaki T, Yokoyama S, EMBO J. 2001 Dec 3;20(23):6612-8. PMID:11726497

Page seeded by OCA on Thu Feb 21 13:02:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1hlv.gif|left|200px]]<br />
+[[Image:1hlv.gif|left|200px]]<br /><applet load="1hlv" size="350" color="white" frame="true" align="right" spinBox="true"
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 caption="1hlv, resolution 2.5&Aring;" />
 '''CRYSTAL STRUCTURE OF CENP-B(1-129) COMPLEXED WITH THE CENP-B BOX DNA'''<br />
 ==Overview==
-The human centromere protein B (CENP-B), one of the centromere components, specifically binds a 17 bp sequence (the CENP-B box), which appears in, every other alpha-satellite repeat. In the present study, the crystal, structure of the complex of the DNA-binding region (129 residues) of, CENP-B and the CENP-B box DNA has been determined at 2.5 A resolution. The, DNA-binding region forms two helix-turn-helix domains, which are bound to, adjacent major grooves of the DNA. The DNA is kinked at the two, recognition helix contact sites, and the DNA region between the kinks is, straight. Among the major groove protein-bound DNAs, this, 'kink-straight-kink' bend contrasts with ordinary 'round bends' (gradual, bending between two protein contact sites). The larger kink (43 degrees ), is induced by a novel mechanism, 'phosphate bridging by an arginine-rich, helix': the recognition helix with an arginine cluster is inserted, perpendicularly into the major groove and bridges the groove through, direct interactions with the phosphate groups. The overall bending angle, is 59 degrees, which may be important for the centromere-specific, chromatin structure.
+The human centromere protein B (CENP-B), one of the centromere components, specifically binds a 17 bp sequence (the CENP-B box), which appears in every other alpha-satellite repeat. In the present study, the crystal structure of the complex of the DNA-binding region (129 residues) of CENP-B and the CENP-B box DNA has been determined at 2.5 A resolution. The DNA-binding region forms two helix-turn-helix domains, which are bound to adjacent major grooves of the DNA. The DNA is kinked at the two recognition helix contact sites, and the DNA region between the kinks is straight. Among the major groove protein-bound DNAs, this 'kink-straight-kink' bend contrasts with ordinary 'round bends' (gradual bending between two protein contact sites). The larger kink (43 degrees ) is induced by a novel mechanism, 'phosphate bridging by an arginine-rich helix': the recognition helix with an arginine cluster is inserted perpendicularly into the major groove and bridges the groove through direct interactions with the phosphate groups. The overall bending angle is 59 degrees, which may be important for the centromere-specific chromatin structure.
 ==About this Structure==
-HLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HLV OCA].
+HLV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HLV OCA].
 ==Reference==
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 [[Category: Nureki, O.]]
 [[Category: Okazaki, T.]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Tanaka, Y.]]
 [[Category: Yokoyama, S.]]
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 [[Category: structural genomics]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:20:03 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:35 2008''