1bhj

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[[Image:1bhj.gif|left|200px]]
[[Image:1bhj.gif|left|200px]]
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{{Structure
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|PDB= 1bhj |SIZE=350|CAPTION= <scene name='initialview01'>1bhj</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1bhj", creates the "Structure Box" on the page.
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|SITE=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glycine_N-methyltransferase Glycine N-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.20 2.1.1.20] </span>
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{{STRUCTURE_1bhj| PDB=1bhj | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhj OCA], [http://www.ebi.ac.uk/pdbsum/1bhj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bhj RCSB]</span>
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'''CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)'''
'''CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)'''
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[[Category: Pattanayek, R.]]
[[Category: Pattanayek, R.]]
[[Category: Wagner, C.]]
[[Category: Wagner, C.]]
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[[Category: folate binding protein]]
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[[Category: Folate binding protein]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:31:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:01:06 2008''
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Revision as of 08:31, 2 May 2008

Image:1bhj.gif

Template:STRUCTURE 1bhj

CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)


Overview

The crystal structure of the recombinant apo-form of glycine N-methyltransferase (GNMT) has been determined at 2.5 A resolution. GNMT is a tetrameric enzyme (monomer Mr = 32,423Da, 292 amino acids) that catalyzes the transfer of a methyl group from S-adenosylmethionine (AdoMet) to glycine with the formation of S-adenosylhomocysteine (AdoHcy) and sarcosine (N-methylglycine). GNMT is a regulatory enzyme, which is inhibited by 5-methyltetrahydrofolate pentaglutamate and believed to control the ratio of AdoMet to AdoHcy in tissues. The crystals belong to the orthorhombic space group P2(1)2(1)2 (a = 85.39, b = 174.21, c = 44.71 A) and contain one dimer per asymmetric unit. The AdoMet-GNMT structure served as the starting model. The structure was refined to an R-factor of 21.9%. Each monomer is a three-domain structure with a large cavity enclosed by the three domains. The tetramer resembles a square with a central channel about which N-terminal domains are intertwined. Only localized changes of the residues involved in the binding pocket are observed for the apo-GNMT structure when compared to that determined in the presence of substrate and substrate analog.

About this Structure

1BHJ is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of apo-glycine N-methyltransferase (GNMT)., Pattanayek R, Newcomer ME, Wagner C, Protein Sci. 1998 Jun;7(6):1326-31. PMID:9655336 Page seeded by OCA on Fri May 2 11:31:23 2008

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