1z5o
From Proteopedia
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- | [[Image:1z5o.gif|left|200px]] | + | [[Image:1z5o.gif|left|200px]] |
- | + | ||
- | '''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine''' | + | {{Structure |
+ | |PDB= 1z5o |SIZE=350|CAPTION= <scene name='initialview01'>1z5o</scene>, resolution 2.00Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=MTA:5'-DEOXY-5'-METHYLTHIOADENOSINE'>MTA</scene> | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Adenosylhomocysteine_nucleosidase Adenosylhomocysteine nucleosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.2.9 3.2.2.9] | ||
+ | |GENE= mtnN, mtn, pfs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1Z5O is a [ | + | 1Z5O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5O OCA]. |
==Reference== | ==Reference== | ||
- | Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis., Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL, J Mol Biol. 2005 Sep 23;352(3):559-74. PMID:[http:// | + | Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis., Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL, J Mol Biol. 2005 Sep 23;352(3):559-74. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16109423 16109423] |
[[Category: Adenosylhomocysteine nucleosidase]] | [[Category: Adenosylhomocysteine nucleosidase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
- | ''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 15:31:29 2008'' |
Revision as of 13:31, 20 March 2008
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, resolution 2.00Å | |||||||
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Ligands: | |||||||
Gene: | mtnN, mtn, pfs (Escherichia coli) | ||||||
Activity: | Adenosylhomocysteine nucleosidase, with EC number 3.2.2.9 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Crystal structure of MTA/AdoHcy nucleosidase Asp197Asn mutant complexed with 5'-methylthioadenosine
Overview
MTA/AdoHcy nucleosidase (MTAN) irreversibly hydrolyzes the N9-C1' bond in the nucleosides, 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (AdoHcy) to form adenine and the corresponding thioribose. MTAN plays a vital role in metabolic pathways involving methionine recycling, biological methylation, polyamine biosynthesis, and quorum sensing. Crystal structures of a wild-type (WT) MTAN complexed with glycerol, and mutant-enzyme and mutant-product complexes have been determined at 2.0A, 2.0A, and 2.1A resolution, respectively. The WT MTAN-glycerol structure provides a purine-free model and in combination with the previously solved thioribose-free MTAN-ADE structure, we now have separate apo structures for both MTAN binding subsites. The purine and thioribose-free states reveal an extensive enzyme-immobilized water network in their respective binding subsites. The Asp197Asn MTAN-MTA and Glu12Gln MTAN-MTR.ADE structures are the first enzyme-substrate and enzyme-product complexes reported for MTAN, respectively. These structures provide representative snapshots along the reaction coordinate and allow insight into the conformational changes of the enzyme and the nucleoside substrate. A "catalytic movie" detailing substrate binding, catalysis, and product release is presented.
About this Structure
1Z5O is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis., Lee JE, Smith GD, Horvatin C, Huang DJ, Cornell KA, Riscoe MK, Howell PL, J Mol Biol. 2005 Sep 23;352(3):559-74. PMID:16109423
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