1wzu
From Proteopedia
(New page: 200px<br /><applet load="1wzu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wzu, resolution 2.0Å" /> '''Crystal structure of ...) |
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| - | [[Image:1wzu.gif|left|200px]]<br /><applet load="1wzu" size=" | + | [[Image:1wzu.gif|left|200px]]<br /><applet load="1wzu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1wzu, resolution 2.0Å" /> | caption="1wzu, resolution 2.0Å" /> | ||
'''Crystal structure of quinolinate synthase (nadA)'''<br /> | '''Crystal structure of quinolinate synthase (nadA)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A gene encoding a quinolinate synthase has been identified in the | + | A gene encoding a quinolinate synthase has been identified in the hyperthermophilic archaeon Pyrococcus horikoshii via genome sequencing. The gene was overexpressed in Escherichia coli, and the crystal structure of the produced enzyme was determined to 2.0 A resolution in the presence of malate, a substrate analogue. The overall structure exhibits a unique triangular architecture composed of a 3-fold repeat of three-layer (alphabetaalpha) sandwich folding. Although some aspects of the fold homologous to the each domain have been observed previously, the overall structure of quinolinate synthase shows no similarity to any known protein structure. The three analogous domains are related to a pseudo-3-fold symmetry. The active site is located at the interface of the three domains and is centered on the pseudo-3-fold axis. The malate molecule is tightly held near the bottom of the active site cavity. The model of the catalytic state during the first condensation step of the quinolinate synthase reaction indicates that the elimination of inorganic phosphate from dihydroxyacetone phosphate may precede the condensation reaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1WZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with MLT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1WZU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_horikoshii Pyrococcus horikoshii] with <scene name='pdbligand=MLT:'>MLT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: nad]] | [[Category: nad]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:49:43 2008'' |
Revision as of 13:49, 21 February 2008
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Crystal structure of quinolinate synthase (nadA)
Overview
A gene encoding a quinolinate synthase has been identified in the hyperthermophilic archaeon Pyrococcus horikoshii via genome sequencing. The gene was overexpressed in Escherichia coli, and the crystal structure of the produced enzyme was determined to 2.0 A resolution in the presence of malate, a substrate analogue. The overall structure exhibits a unique triangular architecture composed of a 3-fold repeat of three-layer (alphabetaalpha) sandwich folding. Although some aspects of the fold homologous to the each domain have been observed previously, the overall structure of quinolinate synthase shows no similarity to any known protein structure. The three analogous domains are related to a pseudo-3-fold symmetry. The active site is located at the interface of the three domains and is centered on the pseudo-3-fold axis. The malate molecule is tightly held near the bottom of the active site cavity. The model of the catalytic state during the first condensation step of the quinolinate synthase reaction indicates that the elimination of inorganic phosphate from dihydroxyacetone phosphate may precede the condensation reaction.
About this Structure
1WZU is a Single protein structure of sequence from Pyrococcus horikoshii with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of the NAD biosynthetic enzyme quinolinate synthase., Sakuraba H, Tsuge H, Yoneda K, Katunuma N, Ohshima T, J Biol Chem. 2005 Jul 22;280(29):26645-8. Epub 2005 Jun 3. PMID:15937336
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