1cbk: Difference between revisions

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[[Image:1cbk.~~gif~~|left|200px]]

[[Image:1cbk.png|left|200px]]

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

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

~~==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~~.

The line below this paragraph, {{ABSTRACT_PUBMED_10080886}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10080886 is the PubMed ID number.

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==About this Structure==

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[[Category: Oefner, C.]]

[[Category: Pyrophosphokinase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 12~~:33:15 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:31:01 2008''

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-[[Image:1cbk.gif|left|200px]]
+{{Seed}}
+[[Image:1cbk.png|left|200px]]
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 {{STRUCTURE_1cbk|  PDB=1cbk  |  SCENE=  }}
-'''7,8-DIHYDRO-6-HYDROXYMETHYLPTERIN-PYROPHOSPHOKINASE FROM HAEMOPHILUS INFLUENZAE'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10080886}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10080886 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10080886}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Oefner, C.]]
 [[Category: Pyrophosphokinase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:33:15 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:31:01 2008''