This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2nad

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nad.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2nad.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nad| PDB=2nad | SCENE= }}
{{STRUCTURE_2nad| PDB=2nad | SCENE= }}
-
'''HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE'''
+
===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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8114093}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8114093 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8114093}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Popov, V O.]]
[[Category: Popov, V O.]]
[[Category: Wilson, K S.]]
[[Category: Wilson, K S.]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:35:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 00:04:02 2008''

Revision as of 21:04, 27 July 2008

Image:2nad.png

Template:STRUCTURE 2nad

HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE

Template:ABSTRACT PUBMED 8114093

About this Structure

2NAD 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 Mon Jul 28 00:04:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nad"
Personal tools