1z5p
From Proteopedia
(New page: 200px<br /><applet load="1z5p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z5p, resolution 2.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1z5p.gif|left|200px]]<br /><applet load="1z5p" size=" | + | [[Image:1z5p.gif|left|200px]]<br /><applet load="1z5p" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1z5p, resolution 2.00Å" /> | caption="1z5p, resolution 2.00Å" /> | ||
'''Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site'''<br /> | '''Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site'''<br /> | ||
==Overview== | ==Overview== | ||
| - | MTA/AdoHcy nucleosidase (MTAN) irreversibly hydrolyzes the N9-C1' bond in | + | 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== | ==About this Structure== | ||
| - | 1Z5P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PE5, GOL and IPA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1Z5P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PE5:'>PE5</scene>, <scene name='pdbligand=GOL:'>GOL</scene> and <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z5P OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cornell, K | + | [[Category: Cornell, K A.]] |
[[Category: Horvatin, C.]] | [[Category: Horvatin, C.]] | ||
| - | [[Category: Howell, P | + | [[Category: Howell, P L.]] |
| - | [[Category: Huang, D | + | [[Category: Huang, D J.T.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J E.]] |
| - | [[Category: Riscoe, M | + | [[Category: Riscoe, M K.]] |
| - | [[Category: Smith, G | + | [[Category: Smith, G D.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: IPA]] | [[Category: IPA]] | ||
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[[Category: mixed alpha/beta]] | [[Category: mixed alpha/beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:17 2008'' |
Revision as of 14:12, 21 February 2008
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Crystal structure of MTA/AdoHcy nucleosidase with a ligand-free purine binding site
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
1Z5P is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Adenosylhomocysteine nucleosidase, with EC number 3.2.2.9 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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