1yf2

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(New page: 200px<br /><applet load="1yf2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yf2, resolution 2.40&Aring;" /> '''Three-dimensional st...)
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'''Three-dimensional structure of DNA sequence specificity (S) subunit of a type I restriction-modification enzyme and its functional implications'''<br />
'''Three-dimensional structure of DNA sequence specificity (S) subunit of a type I restriction-modification enzyme and its functional implications'''<br />
==Overview==
==Overview==
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Type I restriction-modification enzymes are differentiated from type II, and type III enzymes by their recognition of two specific dsDNA sequences, separated by a given spacer and cleaving DNA randomly away from the, recognition sites. They are oligomeric proteins formed by three subunits:, a specificity subunit, a methylation subunit, and a restriction subunit., We solved the crystal structure of a specificity subunit from, Methanococcus jannaschii at 2.4-A resolution. Two highly conserved regions, (CRs) in the middle and at the C terminus form a coiled-coil of long, antiparallel alpha-helices. Two target recognition domains form globular, structures with almost identical topologies and two separate DNA binding, clefts with a modeled DNA helix axis positioned across the CR helices. The, structure suggests that the coiled-coil CRs act as a molecular ruler for, the separation between two recognized DNA sequences. Furthermore, the, relative orientation of the two DNA binding clefts suggests kinking of, bound dsDNA and exposing of target adenines from the recognized DNA, sequences.
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Type I restriction-modification enzymes are differentiated from type II and type III enzymes by their recognition of two specific dsDNA sequences separated by a given spacer and cleaving DNA randomly away from the recognition sites. They are oligomeric proteins formed by three subunits: a specificity subunit, a methylation subunit, and a restriction subunit. We solved the crystal structure of a specificity subunit from Methanococcus jannaschii at 2.4-A resolution. Two highly conserved regions (CRs) in the middle and at the C terminus form a coiled-coil of long antiparallel alpha-helices. Two target recognition domains form globular structures with almost identical topologies and two separate DNA binding clefts with a modeled DNA helix axis positioned across the CR helices. The structure suggests that the coiled-coil CRs act as a molecular ruler for the separation between two recognized DNA sequences. Furthermore, the relative orientation of the two DNA binding clefts suggests kinking of bound dsDNA and exposing of target adenines from the recognized DNA sequences.
==About this Structure==
==About this Structure==
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1YF2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_dsm_2661 Methanocaldococcus jannaschii dsm 2661]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YF2 OCA].
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1YF2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii_dsm_2661 Methanocaldococcus jannaschii dsm 2661]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YF2 OCA].
==Reference==
==Reference==
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[[Category: Methanocaldococcus jannaschii dsm 2661]]
[[Category: Methanocaldococcus jannaschii dsm 2661]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Adams, P.D.]]
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[[Category: Adams, P D.]]
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[[Category: BSGC, Berkeley.Structural.Genomics.Center.]]
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[[Category: BSGC, Berkeley Structural Genomics Center.]]
[[Category: Degiovanni, A.]]
[[Category: Degiovanni, A.]]
[[Category: Jancarik, J.]]
[[Category: Jancarik, J.]]
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[[Category: Kim, J.S.]]
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[[Category: Kim, J S.]]
[[Category: Kim, R.]]
[[Category: Kim, R.]]
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[[Category: Kim, S.H.]]
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[[Category: Kim, S H.]]
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[[Category: Yokota, H.A.]]
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[[Category: Yokota, H A.]]
[[Category: berkeley structural genomics center]]
[[Category: berkeley structural genomics center]]
[[Category: bsgc]]
[[Category: bsgc]]
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[[Category: type i restriction modification enzyme]]
[[Category: type i restriction modification enzyme]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:43:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:04:40 2008''

Revision as of 14:04, 21 February 2008


1yf2, resolution 2.40Å

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Three-dimensional structure of DNA sequence specificity (S) subunit of a type I restriction-modification enzyme and its functional implications

Overview

Type I restriction-modification enzymes are differentiated from type II and type III enzymes by their recognition of two specific dsDNA sequences separated by a given spacer and cleaving DNA randomly away from the recognition sites. They are oligomeric proteins formed by three subunits: a specificity subunit, a methylation subunit, and a restriction subunit. We solved the crystal structure of a specificity subunit from Methanococcus jannaschii at 2.4-A resolution. Two highly conserved regions (CRs) in the middle and at the C terminus form a coiled-coil of long antiparallel alpha-helices. Two target recognition domains form globular structures with almost identical topologies and two separate DNA binding clefts with a modeled DNA helix axis positioned across the CR helices. The structure suggests that the coiled-coil CRs act as a molecular ruler for the separation between two recognized DNA sequences. Furthermore, the relative orientation of the two DNA binding clefts suggests kinking of bound dsDNA and exposing of target adenines from the recognized DNA sequences.

About this Structure

1YF2 is a Single protein structure of sequence from Methanocaldococcus jannaschii dsm 2661. Full crystallographic information is available from OCA.

Reference

Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications., Kim JS, DeGiovanni A, Jancarik J, Adams PD, Yokota H, Kim R, Kim SH, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3248-53. Epub 2005 Feb 22. PMID:15728358

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