1jen
From Proteopedia
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'''HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE''' | '''HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE''' | ||
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[[Category: Pegg, A E.]] | [[Category: Pegg, A E.]] | ||
[[Category: Stanley, B A.]] | [[Category: Stanley, B A.]] | ||
| - | [[Category: | + | [[Category: Allosteric enzyme]] |
| - | [[Category: | + | [[Category: Gene duplication]] |
| - | [[Category: | + | [[Category: Polyamine biosynthesis]] |
| - | [[Category: | + | [[Category: Pyruvoyl]] |
| - | [[Category: | + | [[Category: S-adenosylmethionine decarboxylase]] |
| - | [[Category: | + | [[Category: Sandwich]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 18:07, 2 May 2008
HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE
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.
About this Structure
1JEN is a Protein complex structure of sequences from Homo sapiens. 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 Fri May 2 21:07:51 2008
