1kku

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(New page: 200px<br /> <applet load="1kku" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kku, resolution 2.5&Aring;" /> '''Crystal structure of...)
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'''Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase'''<br />
'''Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase'''<br />
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==About this Structure==
==About this Structure==
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1KKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA].
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1KKU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Nicotinamide-nucleotide_adenylyltransferase Nicotinamide-nucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.1 2.7.7.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KKU OCA].
==Reference==
==Reference==
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[[Category: alpha/beta structure - rossmann fold]]
[[Category: alpha/beta structure - rossmann fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:51:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:14:23 2008''

Revision as of 14:14, 15 February 2008


1kku, resolution 2.5Å

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Crystal structure of nuclear human nicotinamide mononucleotide adenylyltransferase

Overview

Nicotinamide mononucleotide adenylyltransferase (NMNAT), a member of the, nucleotidyltransferase alpha/beta-phosphodiesterases superfamily, catalyzes a universal step (NMN + ATP = NAD + PP(i)) in NAD biosynthesis., Localized within the nucleus, the activity of the human enzyme is greatly, altered in tumor cells, rendering it a promising target for cancer, chemotherapy. By using a combination of single isomorphous replacement and, density modification techniques, the human NMNAT structure was solved by, x-ray crystallography to a 2.5-A resolution, revealing a hexamer that is, composed of alpha/beta-topology subunits. The active site topology of the, enzyme, analyzed through homology modeling and structural comparison with, other NMNATs, yielded convincing evidence for a substrate-induced, conformational change. We also observed remarkable structural conservation, in the ATP-recognition motifs GXXXPX(T/H)XXH and SXTXXR, which we take to, be the universal signature for NMNATs. Structural comparison of human and, prokaryotic NMNATs may also lead to the rational design of highly, selective antimicrobial drugs.

About this Structure

1KKU is a Single protein structure of sequence from Homo sapiens. Active as Nicotinamide-nucleotide adenylyltransferase, with EC number 2.7.7.1 Full crystallographic information is available from OCA.

Reference

Structure of human NMN adenylyltransferase. A key nuclear enzyme for NAD homeostasis., Garavaglia S, D'Angelo I, Emanuelli M, Carnevali F, Pierella F, Magni G, Rizzi M, J Biol Chem. 2002 Mar 8;277(10):8524-30. Epub 2001 Dec 19. PMID:11751893

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