1yt5
From Proteopedia
(New page: 200px<br /><applet load="1yt5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yt5, resolution 2.3Å" /> '''Crystal structure of ...) |
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| - | [[Image:1yt5.gif|left|200px]]<br /><applet load="1yt5" size=" | + | [[Image:1yt5.gif|left|200px]]<br /><applet load="1yt5" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yt5, resolution 2.3Å" /> | caption="1yt5, resolution 2.3Å" /> | ||
'''Crystal structure of NAD kinase from Thermotoga maritima'''<br /> | '''Crystal structure of NAD kinase from Thermotoga maritima'''<br /> | ||
==Overview== | ==Overview== | ||
| - | NAD kinase is the only known enzyme that catalyzes the formation of NADP, a coenzyme involved in most anabolic reactions and in the antioxidant | + | NAD kinase is the only known enzyme that catalyzes the formation of NADP, a coenzyme involved in most anabolic reactions and in the antioxidant defense system. Despite its importance, very little is known regarding the mechanism of catalysis and only recently have several NAD kinase structures been deposited in the PDB. Here, an independent investigation of the crystal structure of inorganic polyphosphate/ATP-NAD kinase, PPNK_THEMA, a protein from Thermotoga maritima, is reported at a resolution of 2.3 A. The crystal structure was solved using single-wavelength anomalous diffraction (SAD) data collected at the Se absorption-peak wavelength in a state in which no cofactors or substrates were bound. It revealed that the 258-amino-acid protein is folded into two distinct domains, similar to recently reported NAD kinases. The N-terminal alpha/beta-domain spans the first 100 amino acids and the last 30 amino acids of the polypeptide and has several topological matches in the PDB, whereas the other domain, which spans the middle 130 residues, adopts a unique beta-sandwich architecture and only appreciably matches the recently deposited PDB structures of NAD kinases. |
==About this Structure== | ==About this Structure== | ||
| - | 1YT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NAD(+)_kinase NAD(+) kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.23 2.7.1.23] Full crystallographic information is available from [http:// | + | 1YT5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/NAD(+)_kinase NAD(+) kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.23 2.7.1.23] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YT5 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution., Oganesyan V, Huang C, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH, Acta | + | Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution., Oganesyan V, Huang C, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):640-6. Epub 2005 Jun 30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16511117 16511117] |
[[Category: NAD(+) kinase]] | [[Category: NAD(+) kinase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermotoga maritima]] | [[Category: Thermotoga maritima]] | ||
| - | [[Category: BSGC, Berkeley | + | [[Category: BSGC, Berkeley Structural Genomics Center.]] |
[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: berkeley structural genomics center]] | [[Category: berkeley structural genomics center]] | ||
| Line 23: | Line 23: | ||
[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:49 2008'' |
Revision as of 14:08, 21 February 2008
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Crystal structure of NAD kinase from Thermotoga maritima
Overview
NAD kinase is the only known enzyme that catalyzes the formation of NADP, a coenzyme involved in most anabolic reactions and in the antioxidant defense system. Despite its importance, very little is known regarding the mechanism of catalysis and only recently have several NAD kinase structures been deposited in the PDB. Here, an independent investigation of the crystal structure of inorganic polyphosphate/ATP-NAD kinase, PPNK_THEMA, a protein from Thermotoga maritima, is reported at a resolution of 2.3 A. The crystal structure was solved using single-wavelength anomalous diffraction (SAD) data collected at the Se absorption-peak wavelength in a state in which no cofactors or substrates were bound. It revealed that the 258-amino-acid protein is folded into two distinct domains, similar to recently reported NAD kinases. The N-terminal alpha/beta-domain spans the first 100 amino acids and the last 30 amino acids of the polypeptide and has several topological matches in the PDB, whereas the other domain, which spans the middle 130 residues, adopts a unique beta-sandwich architecture and only appreciably matches the recently deposited PDB structures of NAD kinases.
About this Structure
1YT5 is a Single protein structure of sequence from Thermotoga maritima with as ligand. Active as NAD(+) kinase, with EC number 2.7.1.23 Full crystallographic information is available from OCA.
Reference
Structure of a NAD kinase from Thermotoga maritima at 2.3 A resolution., Oganesyan V, Huang C, Adams PD, Jancarik J, Yokota HA, Kim R, Kim SH, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):640-6. Epub 2005 Jun 30. PMID:16511117
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