1jen
From Proteopedia
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| - | [[Image:1jen.jpg|left|200px]] | + | [[Image:1jen.jpg|left|200px]] |
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| - | '''HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE''' | + | {{Structure |
| + | |PDB= 1jen |SIZE=350|CAPTION= <scene name='initialview01'>1jen</scene>, resolution 2.250Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenosylmethionine_decarboxylase Adenosylmethionine decarboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.50 4.1.1.50] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HUMAN S-ADENOSYLMETHIONINE DECARBOXYLASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JEN is a [ | + | 1JEN is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEN OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10378277 10378277] |
[[Category: Adenosylmethionine decarboxylase]] | [[Category: Adenosylmethionine decarboxylase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: sandwich]] | [[Category: sandwich]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:02:31 2008'' |
Revision as of 10:02, 20 March 2008
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| , resolution 2.250Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Adenosylmethionine decarboxylase, with EC number 4.1.1.50 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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