1jen
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1jen" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jen, resolution 2.250Å" /> '''HUMAN S-ADENOSYLME...)
Next diff →
Revision as of 15:33, 12 November 2007
|
HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE
Contents |
Overview
BACKGROUND: S-Adenosylmethionine decarboxylase (AdoMetDC) is a critical, regulatory enzyme of the polyamine synthetic pathway, and a well-studied, drug target. The AdoMetDC decarboxylation reaction depends upon a pyruvoyl, cofactor generated via an intramolecular proenzyme self-cleavage reaction., Both the proenzyme-processing and substrate-decarboxylation reactions are, allosterically enhanced by putrescine. Structural elucidation of this, enzyme is necessary to fully interpret the existing mutational and, inhibitor-binding data, and to suggest further experimental studies., RESULTS: The structure of human AdoMetDC has been determined to 2.25 A, resolution using multiwavelength anomalous diffraction (MAD) phasing, methods based on 22 selenium-atom positions. The quaternary structure of, the mature AdoMetDC is an (alpha beta)2 dimer, where alpha and beta, represent the products of the proenzyme self-cleavage reaction. The, architecture of each (alpha beta) monomer is a novel four-layer, alpha/beta-sandwich fold, comprised of two antiparallel eight-stranded, beta sheets flanked by several alpha and 3(10) helices. CONCLUSIONS: The, structure and topology of AdoMetDC display internal symmetry, suggesting, that this protein may be the product of an ancient gene duplication. The, positions of conserved, functionally important residues suggest the, location of the active site and a possible binding site for the effector, molecule putrescine.
Disease
Known disease associated with this structure: Acromesomelic dysplasia, Maroteaux type OMIM:[108961]
About this Structure
1JEN is a Protein complex structure of sequences from Homo sapiens. Active as Adenosylmethionine decarboxylase, with EC number 4.1.1.50 Full crystallographic information is available from OCA.
Reference
The crystal structure of human S-adenosylmethionine decarboxylase at 2.25 A resolution reveals a novel fold., Ekstrom JL, Mathews II, Stanley BA, Pegg AE, Ealick SE, Structure. 1999 May;7(5):583-95. PMID:10378277
Page seeded by OCA on Mon Nov 12 17:40:07 2007
