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1cbk

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(New page: 200px<br /><applet load="1cbk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cbk, resolution 2.02&Aring;" /> '''7,8-DIHYDRO-6-HYDROX...)
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[[Image:1cbk.gif|left|200px]]<br /><applet load="1cbk" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1cbk, resolution 2.02&Aring;" />
'''7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE FROM HAEMOPHILUS INFLUENZAE'''<br />
'''7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE FROM HAEMOPHILUS INFLUENZAE'''<br />
==Overview==
==Overview==
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The gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, of Haemophilus influenzae has been cloned and expressed in Escherichia, coli. A complex of the purified protein with a substrate analog has been, crystallized and its structure solved by multiple anomalous dispersion, using phase information obtained from a single crystal of, selenomethione-labeled protein. The enzyme folds into a four-stranded, antiparallel beta-sheet flanked on one side by two alpha-helices and on, the other by three consecutive alpha-helices, giving a novel, beta1alpha1beta2beta3alpha2beta4alpha3alpha4alpha5 polypeptide topology., The three-dimensional structure of a binary complex has been refined at, 2.1 A resolution. The location of the substrate analog and a sulfate ion, gives important insight into the molecular mechanism of the enzyme.
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The gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase of Haemophilus influenzae has been cloned and expressed in Escherichia coli. A complex of the purified protein with a substrate analog has been crystallized and its structure solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethione-labeled protein. The enzyme folds into a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices and on the other by three consecutive alpha-helices, giving a novel beta1alpha1beta2beta3alpha2beta4alpha3alpha4alpha5 polypeptide topology. The three-dimensional structure of a binary complex has been refined at 2.1 A resolution. The location of the substrate analog and a sulfate ion gives important insight into the molecular mechanism of the enzyme.
==About this Structure==
==About this Structure==
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1CBK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with SO4 and ROI as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CBK OCA].
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1CBK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Haemophilus_influenzae Haemophilus influenzae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ROI:'>ROI</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CBK OCA].
==Reference==
==Reference==
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[[Category: Haemophilus influenzae]]
[[Category: Haemophilus influenzae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Arcy, A.D.]]
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[[Category: Arcy, A D.]]
[[Category: Dale, G.]]
[[Category: Dale, G.]]
[[Category: Hennig, M.]]
[[Category: Hennig, M.]]
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[[Category: pyrophosphokinase]]
[[Category: pyrophosphokinase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 12:19:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:04:24 2008''

Revision as of 10:04, 21 February 2008


1cbk, resolution 2.02Å

Drag the structure with the mouse to rotate

7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE FROM HAEMOPHILUS INFLUENZAE

Overview

The gene encoding the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase of Haemophilus influenzae has been cloned and expressed in Escherichia coli. A complex of the purified protein with a substrate analog has been crystallized and its structure solved by multiple anomalous dispersion using phase information obtained from a single crystal of selenomethione-labeled protein. The enzyme folds into a four-stranded antiparallel beta-sheet flanked on one side by two alpha-helices and on the other by three consecutive alpha-helices, giving a novel beta1alpha1beta2beta3alpha2beta4alpha3alpha4alpha5 polypeptide topology. The three-dimensional structure of a binary complex has been refined at 2.1 A resolution. The location of the substrate analog and a sulfate ion gives important insight into the molecular mechanism of the enzyme.

About this Structure

1CBK is a Single protein structure of sequence from Haemophilus influenzae with and as ligands. Full crystallographic information is available from OCA.

Reference

The structure and function of the 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase from Haemophilus influenzae., Hennig M, Dale GE, D'arcy A, Danel F, Fischer S, Gray CP, Jolidon S, Muller F, Page MG, Pattison P, Oefner C, J Mol Biol. 1999 Mar 26;287(2):211-9. PMID:10080886

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