1hcr
From Proteopedia
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| - | [[Image:1hcr.jpg|left|200px]] | + | [[Image:1hcr.jpg|left|200px]] |
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| - | '''HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS''' | + | {{Structure |
| + | |PDB= 1hcr |SIZE=350|CAPTION= <scene name='initialview01'>1hcr</scene>, resolution 2.300Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HCR is a [ | + | 1HCR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HCR OCA]. |
==Reference== | ==Reference== | ||
| - | Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions., Feng JA, Johnson RC, Dickerson RE, Science. 1994 Jan 21;263(5145):348-55. PMID:[http:// | + | Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions., Feng JA, Johnson RC, Dickerson RE, Science. 1994 Jan 21;263(5145):348-55. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8278807 8278807] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dickerson, R E.]] | [[Category: Dickerson, R E.]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:35:22 2008'' |
Revision as of 09:35, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
HIN RECOMBINASE BOUND TO DNA: THE ORIGIN OF SPECIFICITY IN MAJOR AND MINOR GROOVE INTERACTIONS
Overview
The structure of the 52-amino acid DNA-binding domain of the prokaryotic Hin recombinase, complexed with a DNA recombination half-site, has been solved by x-ray crystallography at 2.3 angstrom resolution. The Hin domain consists of a three-alpha-helix bundle, with the carboxyl-terminal helix inserted into the major groove of DNA, and two flanking extended polypeptide chains that contact bases in the minor groove. The overall structure displays features resembling both a prototypical bacterial helix-turn-helix and the eukaryotic homeodomain, and in many respects is an intermediate between these two DNA-binding motifs. In addition, a new structural motif is seen: the six-amino acid carboxyl-terminal peptide of the Hin domain runs along the minor groove at the edge of the recombination site, with the peptide backbone facing the floor of the groove and side chains extending away toward the exterior. The x-ray structure provides an almost complete explanation for DNA mutant binding studies in the Hin system and for DNA specificity observed in the Hin-related family of DNA invertases.
About this Structure
1HCR is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Hin recombinase bound to DNA: the origin of specificity in major and minor groove interactions., Feng JA, Johnson RC, Dickerson RE, Science. 1994 Jan 21;263(5145):348-55. PMID:8278807
Page seeded by OCA on Thu Mar 20 11:35:22 2008
