2nac

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:2nac.jpg|left|200px]]
[[Image:2nac.jpg|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 2nac |SIZE=350|CAPTION= <scene name='initialview01'>2nac</scene>, resolution 1.80&Aring;
+
The line below this paragraph, containing "STRUCTURE_2nac", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Formate_dehydrogenase Formate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.2 1.2.1.2] </span>
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_2nac| PDB=2nac | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nac OCA], [http://www.ebi.ac.uk/pdbsum/2nac PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nac RCSB]</span>
+
-
}}
+
'''HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE'''
'''HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE'''
Line 31: Line 28:
[[Category: Popov, V O.]]
[[Category: Popov, V O.]]
[[Category: Wilson, K S.]]
[[Category: Wilson, K S.]]
-
[[Category: oxidoreductase(aldehyde(d),nad+(a))]]
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:35:18 2008''
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:04:36 2008''
+

Revision as of 06:35, 4 May 2008

Template:STRUCTURE 2nac

HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE


Overview

Three-dimensional crystal structures of holo (ternary complex enzyme-NAD-azide) and apo NAD-dependent dimeric formate dehydrogenase (FDH) from the methylotrophic bacterium Pseudomonas sp. 101 have been refined to R factors of 11.7% and 14.8% at 2.05 and 1.80 A resolution, respectively. The estimated root-mean-square error in atomic co-ordinates is 0.11 A for holo and 0.18 A for apo. X-ray data were collected from single crystals using an imaging plate scanner and synchrotron radiation. In both crystal forms there is a dimer in the asymmetric unit. Both structures show essentially 2-fold molecular symmetry. NAD binding causes movement of the catalytic domain and ordering of the C terminus, where a new helix appears. This completes formation of the enzyme active centre in holo FDH. NAD is bound in the cleft separating the domains and mainly interacts with residues from the co-enzyme binding domain. In apo FDH these residues are held in essentially the same conformation by water molecules occupying the NAD binding region. An azide molecule is located near the point of catalysis, the C4 atom of the nicotinamide moiety of NAD, and overlaps with the proposed formate binding site. There is an extensive channel running from the active site to the protein surface and this is supposed to be used by substrate to reach the active centre after NAD has already bound. The structure of the active site and a hypothetical catalytic mechanism are discussed. Sequence homology of FDH with other NAD-dependent formate dehydrogenases and some D-specific dehydrogenases is discussed on the basis of the FDH three-dimensional structure.

About this Structure

2NAC is a Single protein structure of sequence from Pseudomonas sp.. Full crystallographic information is available from OCA.

Reference

High resolution structures of holo and apo formate dehydrogenase., Lamzin VS, Dauter Z, Popov VO, Harutyunyan EH, Wilson KS, J Mol Biol. 1994 Feb 25;236(3):759-85. PMID:8114093 Page seeded by OCA on Sun May 4 09:35:18 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools