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.


1f9a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1f9a.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1f9a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1f9a| PDB=1f9a | SCENE= }}
{{STRUCTURE_1f9a| PDB=1f9a | SCENE= }}
-
'''CRYSTAL STRUCTURE ANALYSIS OF NMN ADENYLYLTRANSFERASE FROM METHANOCOCCUS JANNASCHII'''
+
===CRYSTAL STRUCTURE ANALYSIS OF NMN ADENYLYLTRANSFERASE FROM METHANOCOCCUS JANNASCHII===
-
==Overview==
+
<!--
-
BACKGROUND: Nicotinamide adenine dinucleotide (NAD(+)) is an essential cofactor involved in fundamental processes in cell metabolism. The enzyme nicotinamide mononucleotide adenylyltransferase (NMN AT) plays a key role in NAD(+) biosynthesis, catalysing the condensation of nicotinamide mononucleotide and ATP, and yielding NAD(+) and pyrophosphate. Given its vital role in cell life, the enzyme represents a possible target for the development of new antibacterial agents. RESULTS: The structure of NMN AT from Methanococcus jannaschii in complex with ATP has been solved by X-ray crystallography at 2.0 A resolution, using a combination of single isomorphous replacement and density modification techniques. The structure reveals a hexamer with 32 point group symmetry composed of alpha/beta topology subunits. The catalytic site is located in a deep cleft on the surface of each subunit, where one ATP molecule and one Mg(2+) are observed. A strictly conserved HXGH motif (in single-letter amino acid code) is involved in ATP binding and recognition. CONCLUSIONS: The structure of NMN AT closely resembles that of phosphopantetheine adenylyltransferase. Remarkably, in spite of the fact that the two enzymes share the same fold and hexameric assembly, a striking difference in their quaternary structure is observed. Moreover, on the basis of structural similarity including the HXGH motif, we identify NMN AT as a novel member of the newly proposed superfamily of nucleotidyltransferase alpha/beta phosphodiesterases. Our structural data suggest that the catalytic mechanism does not rely on the direct involvement of any protein residues and is likely to be carried out through optimal positioning of substrates and transition-state stabilisation, as is proposed for other members of the nucleotidyltransferase alpha/beta phosphodiesterase superfamily.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10986466}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10986466 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10986466}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:03:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 02:54:13 2008''

Revision as of 23:54, 30 June 2008

Image:1f9a.png

Template:STRUCTURE 1f9a

CRYSTAL STRUCTURE ANALYSIS OF NMN ADENYLYLTRANSFERASE FROM METHANOCOCCUS JANNASCHII

Template:ABSTRACT PUBMED 10986466

About this Structure

1F9A is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Structure of nicotinamide mononucleotide adenylyltransferase: a key enzyme in NAD(+) biosynthesis., D'Angelo I, Raffaelli N, Dabusti V, Lorenzi T, Magni G, Rizzi M, Structure. 2000 Sep 15;8(9):993-1004. PMID:10986466

Page seeded by OCA on Tue Jul 1 02:54:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1f9a"
Personal tools