1lwa
From Proteopedia
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| - | [[Image:1lwa.gif|left|200px]] | + | [[Image:1lwa.gif|left|200px]] |
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| - | '''Solution Structure of SRY_DNA''' | + | {{Structure |
| + | |PDB= 1lwa |SIZE=350|CAPTION= <scene name='initialview01'>1lwa</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Solution Structure of SRY_DNA''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LWA is a [ | + | 1LWA is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWA OCA]. |
==Reference== | ==Reference== | ||
| - | The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding., Masse JE, Wong B, Yen YM, Allain FH, Johnson RC, Feigon J, J Mol Biol. 2002 Oct 18;323(2):263-84. PMID:[http:// | + | The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding., Masse JE, Wong B, Yen YM, Allain FH, Johnson RC, Feigon J, J Mol Biol. 2002 Oct 18;323(2):263-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12381320 12381320] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Allain, F H.T.]] | [[Category: Allain, F H.T.]] | ||
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[[Category: double-stranded dna]] | [[Category: double-stranded dna]] | ||
| - | ''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 12:35:58 2008'' |
Revision as of 10:36, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of SRY_DNA
Overview
NHP6A is a non-sequence-specific DNA-binding protein from Saccharomyces cerevisiae which belongs to the HMGB protein family. Previously, we have solved the structure of NHP6A in the absence of DNA and modeled its interaction with DNA. Here, we present the refined solution structures of the NHP6A-DNA complex as well as the free 15bp DNA. Both the free and bound forms of the protein adopt the typical L-shaped HMGB domain fold. The DNA in the complex undergoes significant structural rearrangement from its free form while the protein shows smaller but significant conformational changes in the complex. Structural and mutational analysis as well as comparison of the complex with the free DNA provides insight into the factors that contribute to binding site selection and DNA deformations in the complex. Further insight into the amino acid determinants of DNA binding by HMGB domain proteins is given by a correlation study of NHP6A and 32 other HMGB domains belonging to both the DNA-sequence-specific and non-sequence-specific families of HMGB proteins. The resulting correlations can be rationalized by comparison of solved structures of HMGB proteins.
About this Structure
1LWA is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding., Masse JE, Wong B, Yen YM, Allain FH, Johnson RC, Feigon J, J Mol Biol. 2002 Oct 18;323(2):263-84. PMID:12381320
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