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1vie

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(New page: 200px<br /><applet load="1vie" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vie, resolution 1.7&Aring;" /> '''STRUCTURE OF DIHYDROF...)
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[[Image:1vie.gif|left|200px]]<br /><applet load="1vie" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1vie, resolution 1.7&Aring;" />
caption="1vie, resolution 1.7&Aring;" />
'''STRUCTURE OF DIHYDROFOLATE REDUCTASE'''<br />
'''STRUCTURE OF DIHYDROFOLATE REDUCTASE'''<br />
==Overview==
==Overview==
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Bacteria expressing R67-plasmid encoded dihydrofolate reductase (R67 DHFR), exhibit high-level resistance to the antibiotic trimethoprim. Native R67, DHFR is a 34,000 M(r) homotetramer which exists in equilibrium with an, inactive dimeric form. The structure of native R67 DHFR has now been, solved at 1.7 A resolution and is unrelated to that of chromosomal DHFR., Homotetrameric R67 DHFR has an unusual pore, 25 A in length, passing, through the middle of the molecule. Two folate molecules bind, asymmetrically within the pore indicating that the enzyme's active site, consists of symmetry related binding surfaces from all four identical, units.
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Bacteria expressing R67-plasmid encoded dihydrofolate reductase (R67 DHFR) exhibit high-level resistance to the antibiotic trimethoprim. Native R67 DHFR is a 34,000 M(r) homotetramer which exists in equilibrium with an inactive dimeric form. The structure of native R67 DHFR has now been solved at 1.7 A resolution and is unrelated to that of chromosomal DHFR. Homotetrameric R67 DHFR has an unusual pore, 25 A in length, passing through the middle of the molecule. Two folate molecules bind asymmetrically within the pore indicating that the enzyme's active site consists of symmetry related binding surfaces from all four identical units.
==About this Structure==
==About this Structure==
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1VIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VIE OCA].
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1VIE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Active as [http://en.wikipedia.org/wiki/Dihydrofolate_reductase Dihydrofolate reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.5.1.3 1.5.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VIE OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Howell, E.E.]]
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[[Category: Howell, E E.]]
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[[Category: Matthews, D.A.]]
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[[Category: Matthews, D A.]]
[[Category: Narayana, N.]]
[[Category: Narayana, N.]]
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[[Category: Xuong, N.H.]]
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[[Category: Xuong, N H.]]
[[Category: methotrexate resistance]]
[[Category: methotrexate resistance]]
[[Category: nadp]]
[[Category: nadp]]
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[[Category: trimethoprim resistance]]
[[Category: trimethoprim resistance]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:52:55 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:39 2008''

Revision as of 13:35, 21 February 2008

Image:1vie.gif

1vie, resolution 1.7Å

Drag the structure with the mouse to rotate

STRUCTURE OF DIHYDROFOLATE REDUCTASE

Overview

Bacteria expressing R67-plasmid encoded dihydrofolate reductase (R67 DHFR) exhibit high-level resistance to the antibiotic trimethoprim. Native R67 DHFR is a 34,000 M(r) homotetramer which exists in equilibrium with an inactive dimeric form. The structure of native R67 DHFR has now been solved at 1.7 A resolution and is unrelated to that of chromosomal DHFR. Homotetrameric R67 DHFR has an unusual pore, 25 A in length, passing through the middle of the molecule. Two folate molecules bind asymmetrically within the pore indicating that the enzyme's active site consists of symmetry related binding surfaces from all four identical units.

About this Structure

1VIE is a Single protein structure of sequence from Escherichia coli. Active as Dihydrofolate reductase, with EC number 1.5.1.3 Full crystallographic information is available from OCA.

Reference

A plasmid-encoded dihydrofolate reductase from trimethoprim-resistant bacteria has a novel D2-symmetric active site., Narayana N, Matthews DA, Howell EE, Nguyen-huu X, Nat Struct Biol. 1995 Nov;2(11):1018-25. PMID:7583655

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