1nvt

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1nvt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nvt, resolution 2.35&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:1nvt.gif|left|200px]]<br /><applet load="1nvt" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1nvt.gif|left|200px]]<br /><applet load="1nvt" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nvt, resolution 2.35&Aring;" />
caption="1nvt, resolution 2.35&Aring;" />
'''Crystal structure of Shikimate Dehydrogenase (AROE or MJ1084) in complex with NADP+'''<br />
'''Crystal structure of Shikimate Dehydrogenase (AROE or MJ1084) in complex with NADP+'''<br />
==Overview==
==Overview==
-
The crystal structure of Methanococcus jannaschii shikimate, 5-dehydrogenase (MjSDH) bound to the cofactor nicotinamide adenine, dinucleotide phosphate (NADP) has been determined at 2.35 A resolution., Shikimate 5-dehydrogenase (SDH) is responsible for NADP-dependent, catalysis of the fourth step in shikimate biosynthesis, which is essential, for aromatic amino acid metabolism in bacteria, microbial eukaryotes, and, plants. The structure of MjSDH is a compact alpha/beta sandwich with two, distinct domains, responsible for binding substrate and the NADP cofactor, respectively. A phylogenetically conserved deep cleft on the protein, surface corresponds to the enzyme active site. The structure reveals a, topologically new domain fold within the N-terminal segment of the, polypeptide chain, which binds substrate and supports dimerization., Insights gained from homology modeling and sequence/structure comparisons, suggest that the SDHs represent a unique class of dehydrogenases. The, structure provides a framework for further investigation to discover and, develop novel inhibitors targeting this essential enzyme.
+
The crystal structure of Methanococcus jannaschii shikimate 5-dehydrogenase (MjSDH) bound to the cofactor nicotinamide adenine dinucleotide phosphate (NADP) has been determined at 2.35 A resolution. Shikimate 5-dehydrogenase (SDH) is responsible for NADP-dependent catalysis of the fourth step in shikimate biosynthesis, which is essential for aromatic amino acid metabolism in bacteria, microbial eukaryotes, and plants. The structure of MjSDH is a compact alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively. A phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site. The structure reveals a topologically new domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization. Insights gained from homology modeling and sequence/structure comparisons suggest that the SDHs represent a unique class of dehydrogenases. The structure provides a framework for further investigation to discover and develop novel inhibitors targeting this essential enzyme.
==About this Structure==
==About this Structure==
-
1NVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with ZN and NAP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NVT OCA].
+
1NVT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NAP:'>NAP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NVT OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Shikimate dehydrogenase]]
[[Category: Shikimate dehydrogenase]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Burley, S.K.]]
+
[[Category: Burley, S K.]]
-
[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
+
[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
-
[[Category: Padyana, A.K.]]
+
[[Category: Padyana, A K.]]
[[Category: NAP]]
[[Category: NAP]]
[[Category: ZN]]
[[Category: ZN]]
Line 25: Line 25:
[[Category: structural genomics]]
[[Category: structural genomics]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:35:46 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:10:36 2008''

Revision as of 12:10, 21 February 2008


1nvt, resolution 2.35Å

Drag the structure with the mouse to rotate

Crystal structure of Shikimate Dehydrogenase (AROE or MJ1084) in complex with NADP+

Overview

The crystal structure of Methanococcus jannaschii shikimate 5-dehydrogenase (MjSDH) bound to the cofactor nicotinamide adenine dinucleotide phosphate (NADP) has been determined at 2.35 A resolution. Shikimate 5-dehydrogenase (SDH) is responsible for NADP-dependent catalysis of the fourth step in shikimate biosynthesis, which is essential for aromatic amino acid metabolism in bacteria, microbial eukaryotes, and plants. The structure of MjSDH is a compact alpha/beta sandwich with two distinct domains, responsible for binding substrate and the NADP cofactor, respectively. A phylogenetically conserved deep cleft on the protein surface corresponds to the enzyme active site. The structure reveals a topologically new domain fold within the N-terminal segment of the polypeptide chain, which binds substrate and supports dimerization. Insights gained from homology modeling and sequence/structure comparisons suggest that the SDHs represent a unique class of dehydrogenases. The structure provides a framework for further investigation to discover and develop novel inhibitors targeting this essential enzyme.

About this Structure

1NVT is a Single protein structure of sequence from Methanocaldococcus jannaschii with and as ligands. Active as Shikimate dehydrogenase, with EC number 1.1.1.25 Full crystallographic information is available from OCA.

Reference

Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: insights into function and evolution., Padyana AK, Burley SK, Structure. 2003 Aug;11(8):1005-13. PMID:12906831

Page seeded by OCA on Thu Feb 21 14:10:36 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools