2fl3

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[[Image:2fl3.gif|left|200px]]<br /><applet load="2fl3" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2fl3.gif|left|200px]]
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caption="2fl3, resolution 2.39&Aring;" />
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'''Binary Complex of Restriction Endonuclease HinP1I with Cognate DNA'''<br />
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{{Structure
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|PDB= 2fl3 |SIZE=350|CAPTION= <scene name='initialview01'>2fl3</scene>, resolution 2.39&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY= [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4]
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|GENE= hinP1IR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 Haemophilus influenzae])
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}}
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'''Binary Complex of Restriction Endonuclease HinP1I with Cognate DNA'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2FL3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Active as [http://en.wikipedia.org/wiki/Type_II_site-specific_deoxyribonuclease Type II site-specific deoxyribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.4 3.1.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FL3 OCA].
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2FL3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FL3 OCA].
==Reference==
==Reference==
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DNA nicking by HinP1I endonuclease: bending, base flipping and minor groove expansion., Horton JR, Zhang X, Maunus R, Yang Z, Wilson GG, Roberts RJ, Cheng X, Nucleic Acids Res. 2006 Feb 9;34(3):939-48. Print 2006. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16473850 16473850]
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DNA nicking by HinP1I endonuclease: bending, base flipping and minor groove expansion., Horton JR, Zhang X, Maunus R, Yang Z, Wilson GG, Roberts RJ, Cheng X, Nucleic Acids Res. 2006 Feb 9;34(3):939-48. Print 2006. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16473850 16473850]
[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: restriction endonuclease]]
[[Category: restriction endonuclease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:27 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:53:44 2008''

Revision as of 14:53, 20 March 2008


PDB ID 2fl3

Drag the structure with the mouse to rotate
, resolution 2.39Å
Gene: hinP1IR (Haemophilus influenzae)
Activity: Type II site-specific deoxyribonuclease, with EC number 3.1.21.4
Coordinates: save as pdb, mmCIF, xml



Binary Complex of Restriction Endonuclease HinP1I with Cognate DNA


Overview

HinP1I recognizes and cleaves the palindromic tetranucleotide sequence G downward arrowCGC in DNA. We report three structures of HinP1I-DNA complexes: in the presence of Ca(2+) (pre-reactive complex), in the absence of metal ion (binary complex) and in the presence of Mg(2+) (post-reactive complex). HinP1I forms a back-to-back dimer with two active sites and two DNA duplexes bound on the outer surfaces of the dimer facing away from each other. The 10 bp DNA duplexes undergo protein-induced distortions exhibiting features of A-, B- and Z-conformations: bending on one side (by intercalation of a phenylalanine side chain into the major groove), base flipping on the other side of the recognition site (by expanding the step rise distance of the local base pair to Z-form) and a local A-form conformation between the two central C:G base pairs of the recognition site (by binding of the N-terminal helix in the minor groove). In the pre- and post-reactive complexes, two metals (Ca(2+) or Mg(2+)) are found in the active site. The enzyme appears to cleave DNA sequentially, hydrolyzing first one DNA strand, as seen in the post-reactive complex in the crystalline state, and then the other, as supported by the observation that, in solution, a nicked DNA intermediate accumulates before linearization.

About this Structure

2FL3 is a Single protein structure of sequence from Haemophilus influenzae. Full crystallographic information is available from OCA.

Reference

DNA nicking by HinP1I endonuclease: bending, base flipping and minor groove expansion., Horton JR, Zhang X, Maunus R, Yang Z, Wilson GG, Roberts RJ, Cheng X, Nucleic Acids Res. 2006 Feb 9;34(3):939-48. Print 2006. PMID:16473850

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