1z0u: Difference between revisions

Revision as of 16:22, 27 July 2008

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File:1z0u.png

Template:STRUCTURE 1z0u

Crystal structure of a NAD kinase from Archaeoglobus fulgidus bound by NADPCrystal structure of a NAD kinase from Archaeoglobus fulgidus bound by NADP

Template:ABSTRACT PUBMED 16242716

About this StructureAbout this Structure

1Z0U is a Single protein structure of sequence from Archaeoglobus fulgidus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP., Liu J, Lou Y, Yokota H, Adams PD, Kim R, Kim SH, J Mol Biol. 2005 Nov 25;354(2):289-303. Epub 2005 Sep 30. PMID:16242716

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1z0u.gif|left|200px]]
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-'''Crystal structure of a NAD kinase from Archaeoglobus fulgidus bound by NADP'''
+===Crystal structure of a NAD kinase from Archaeoglobus fulgidus bound by NADP===
-==Overview==
+<!--
-NAD kinase is a ubiquitous enzyme that catalyzes the phosphorylation of NAD to NADP using ATP or inorganic polyphosphate (poly(P)) as phosphate donor, and is regarded as the only enzyme responsible for the synthesis of NADP. We present here the crystal structures of an NAD kinase from the archaeal organism Archaeoglobus fulgidus in complex with its phosphate donor ATP at 1.7 A resolution, with its substrate NAD at 3.05 A resolution, and with the product NADP in two different crystal forms at 2.45 A and 2.0 A resolution, respectively. In the ATP bound structure, the AMP portion of the ATP molecule is found to use the same binding site as the nicotinamide ribose portion of NAD/NADP in the NAD/NADP bound structures. A magnesium ion is found to be coordinated to the phosphate tail of ATP as well as to a pyrophosphate group. The conserved GGDG loop forms hydrogen bonds with the pyrophosphate group in the ATP-bound structure and the 2' phosphate group of the NADP in the NADP-bound structures. A possible phosphate transfer mechanism is proposed on the basis of the structures presented.
+The line below this paragraph, {{ABSTRACT_PUBMED_16242716}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16242716 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16242716}}
 ==About this Structure==
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 [[Category: Psi]]
 [[Category: Structural genomic]]
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