1nc1

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[[Image:1nc1.jpg|left|200px]]
[[Image:1nc1.jpg|left|200px]]
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{{Structure
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|PDB= 1nc1 |SIZE=350|CAPTION= <scene name='initialview01'>1nc1</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1nc1", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=MTH:2-(4-AMINO-PYRROLO[2,3-D]PYRIMIDIN-7-YL)-5-METHYLSULFANYLMETHYL-TETRAHYDRO-FURAN-3,4-DIOL'>MTH</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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|GENE= MTN OR PFS OR B0159 OR Z0170 OR ECS0163 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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{{STRUCTURE_1nc1| PDB=1nc1 | SCENE= }}
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|RELATEDENTRY=[[1jys|1JYS]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nc1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nc1 OCA], [http://www.ebi.ac.uk/pdbsum/1nc1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nc1 RCSB]</span>
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}}
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'''Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)'''
'''Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)'''
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[[Category: Lee, J E.]]
[[Category: Lee, J E.]]
[[Category: Riscoe, M K.]]
[[Category: Riscoe, M K.]]
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[[Category: mixed alpha/beta dimer]]
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[[Category: Mixed alpha/beta dimer]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:21:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:28:15 2008''
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Revision as of 23:21, 2 May 2008

Template:STRUCTURE 1nc1

Crystal structure of E. coli MTA/AdoHcy nucleosidase complexed with 5'-methylthiotubercidin (MTH)


Overview

5'-Methylthioadenosine/S-adenosylhomocysteine (MTA/AdoHcy) nucleosidase is a key enzyme in a number of critical biological processes in many microbes. This nucleosidase catalyzes the irreversible hydrolysis of the N(9)-C(1') bond of MTA or AdoHcy to form adenine and the corresponding thioribose. The key role of the MTA/AdoHcy nucleosidase in biological methylation, polyamine biosynthesis, methionine recycling, and bacterial quorum sensing has made it an important antimicrobial drug target. The crystal structures of Escherichia coli MTA/AdoHcy nucleosidase complexed with the transition state analog, formycin A (FMA), and the nonhydrolyzable substrate analog, 5'-methylthiotubercidin (MTT) have been solved to 2.2- and 2.0-A resolution, respectively. These are the first MTA/AdoHcy nucleosidase structures to be solved in the presence of inhibitors. These structures clearly identify the residues involved in substrate binding and catalysis in the active site. Comparisons of the inhibitor complexes to the adenine-bound MTA/AdoHcy nucleosidase (Lee, J. E., Cornell, K. A., Riscoe, M. K., and Howell, P. L. (2001) Structure (Camb.) 9, 941-953) structure provide evidence for a ligand-induced conformational change in the active site and the substrate preference of the enzyme. The enzymatic mechanism has been re-examined.

About this Structure

1NC1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis., Lee JE, Cornell KA, Riscoe MK, Howell PL, J Biol Chem. 2003 Mar 7;278(10):8761-70. Epub 2002 Dec 20. PMID:12496243 Page seeded by OCA on Sat May 3 02:21:07 2008

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