1z5n
From Proteopedia
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|PDB= 1z5n |SIZE=350|CAPTION= <scene name='initialview01'>1z5n</scene>, resolution 2.10Å | |PDB= 1z5n |SIZE=350|CAPTION= <scene name='initialview01'>1z5n</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SR1:5-S-METHYL-5-THIO-ALPHA-D-RIBOFURANOSE'>SR1</scene> | + | |LIGAND= <scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=SR1:5-S-METHYL-5-THIO-ALPHA-D-RIBOFURANOSE'>SR1</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[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] </span> | |
|GENE= mtnN, mtn, pfs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= mtnN, mtn, pfs ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1z5o|1Z5O]], [[1z5p|1Z5P]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z5n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z5n OCA], [http://www.ebi.ac.uk/pdbsum/1z5n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z5n RCSB]</span> | ||
}} | }} | ||
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[[Category: Riscoe, M K.]] | [[Category: Riscoe, M K.]] | ||
[[Category: Smith, G D.]] | [[Category: Smith, G D.]] | ||
| - | [[Category: ADE]] | ||
| - | [[Category: SR1]] | ||
[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:29:24 2008'' |
Revision as of 22:29, 30 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | mtnN, mtn, pfs (Escherichia coli) | ||||||
| Activity: | Adenosylhomocysteine nucleosidase, with EC number 3.2.2.9 | ||||||
| Related: | 1Z5O, 1Z5P
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of MTA/AdoHcy nucleosidase Glu12Gln mutant complexed with 5-methylthioribose and adenine
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
1Z5N 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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