1l1n

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(New page: 200px<br /><applet load="1l1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l1n, resolution 2.1&Aring;" /> '''POLIOVIRUS 3C PROTEIN...)
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caption="1l1n, resolution 2.1&Aring;" />
'''POLIOVIRUS 3C PROTEINASE'''<br />
'''POLIOVIRUS 3C PROTEINASE'''<br />
==Overview==
==Overview==
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The X-ray crystallographic structure of the recombinant poliovirus 3C gene, product (Mahoney strain) has been determined by single isomorphous, replacement and non-crystallographic symmetry averaging and refined at 2.1, A resolution. Poliovirus 3C is comprised of two six-stranded antiparallel, beta-barrel domains and is structurally similar to the chymotrypsin-like, serine proteinases. The shallow active site cleft is located at the, junction of the two beta-barrel domains and contains a His40, Glu71, Cys147 catalytic triad. The polypeptide loop preceding Cys147 is flexible, and likely undergoes a conformational change upon substrate binding. The, specificity pockets for poliovirus 3C are well-defined and modeling, studies account for the known substrate specificity of this proteinase., Poliovirus 3C also participates in the formation of the viral replicative, initiation complex where it specifically recognizes and binds the RNA, stem-loop structure in the 5' non-translated region of its own genome. The, RNA recognition site of 3C is located on the opposite side of the molecule, in relation to its proteolytic active site and is centered about the, conserved KFRDIR sequence of the domain linker. The recognition site is, well-defined and also includes residues from the amino and, carboxy-terminal helices. The two molecules in the asymmetric unit are, related by an approximate 2-fold, non-crystallographic symmetry and form, an intermolecular antiparallel beta-sheet at their interface.
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The X-ray crystallographic structure of the recombinant poliovirus 3C gene product (Mahoney strain) has been determined by single isomorphous replacement and non-crystallographic symmetry averaging and refined at 2.1 A resolution. Poliovirus 3C is comprised of two six-stranded antiparallel beta-barrel domains and is structurally similar to the chymotrypsin-like serine proteinases. The shallow active site cleft is located at the junction of the two beta-barrel domains and contains a His40, Glu71, Cys147 catalytic triad. The polypeptide loop preceding Cys147 is flexible and likely undergoes a conformational change upon substrate binding. The specificity pockets for poliovirus 3C are well-defined and modeling studies account for the known substrate specificity of this proteinase. Poliovirus 3C also participates in the formation of the viral replicative initiation complex where it specifically recognizes and binds the RNA stem-loop structure in the 5' non-translated region of its own genome. The RNA recognition site of 3C is located on the opposite side of the molecule in relation to its proteolytic active site and is centered about the conserved KFRDIR sequence of the domain linker. The recognition site is well-defined and also includes residues from the amino and carboxy-terminal helices. The two molecules in the asymmetric unit are related by an approximate 2-fold, non-crystallographic symmetry and form an intermolecular antiparallel beta-sheet at their interface.
==About this Structure==
==About this Structure==
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1L1N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1]. Active as [http://en.wikipedia.org/wiki/Picornain_3C Picornain 3C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.28 3.4.22.28] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L1N OCA].
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1L1N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_poliovirus_1 Human poliovirus 1]. Active as [http://en.wikipedia.org/wiki/Picornain_3C Picornain 3C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.28 3.4.22.28] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1N OCA].
==Reference==
==Reference==
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[[Category: Picornain 3C]]
[[Category: Picornain 3C]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chernaia, M.M.]]
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[[Category: Chernaia, M M.]]
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[[Category: James, M.N.G.]]
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[[Category: James, M N.G.]]
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[[Category: Mosimann, S.C.]]
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[[Category: Mosimann, S C.]]
[[Category: Plotch, S.]]
[[Category: Plotch, S.]]
[[Category: Sia, S.]]
[[Category: Sia, S.]]
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[[Category: trypsin-like]]
[[Category: trypsin-like]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:10:14 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:17 2008''

Revision as of 11:40, 21 February 2008


1l1n, resolution 2.1Å

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POLIOVIRUS 3C PROTEINASE

Overview

The X-ray crystallographic structure of the recombinant poliovirus 3C gene product (Mahoney strain) has been determined by single isomorphous replacement and non-crystallographic symmetry averaging and refined at 2.1 A resolution. Poliovirus 3C is comprised of two six-stranded antiparallel beta-barrel domains and is structurally similar to the chymotrypsin-like serine proteinases. The shallow active site cleft is located at the junction of the two beta-barrel domains and contains a His40, Glu71, Cys147 catalytic triad. The polypeptide loop preceding Cys147 is flexible and likely undergoes a conformational change upon substrate binding. The specificity pockets for poliovirus 3C are well-defined and modeling studies account for the known substrate specificity of this proteinase. Poliovirus 3C also participates in the formation of the viral replicative initiation complex where it specifically recognizes and binds the RNA stem-loop structure in the 5' non-translated region of its own genome. The RNA recognition site of 3C is located on the opposite side of the molecule in relation to its proteolytic active site and is centered about the conserved KFRDIR sequence of the domain linker. The recognition site is well-defined and also includes residues from the amino and carboxy-terminal helices. The two molecules in the asymmetric unit are related by an approximate 2-fold, non-crystallographic symmetry and form an intermolecular antiparallel beta-sheet at their interface.

About this Structure

1L1N is a Single protein structure of sequence from Human poliovirus 1. Active as Picornain 3C, with EC number 3.4.22.28 Full crystallographic information is available from OCA.

Reference

Refined X-ray crystallographic structure of the poliovirus 3C gene product., Mosimann SC, Cherney MM, Sia S, Plotch S, James MN, J Mol Biol. 1997 Nov 14;273(5):1032-47. PMID:9367789

Page seeded by OCA on Thu Feb 21 13:40:17 2008

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