3bq5

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[[Image:3bq5.jpg|left|200px]]
[[Image:3bq5.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 3bq5 |SIZE=350|CAPTION= <scene name='initialview01'>3bq5</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_3bq5", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+800'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+801'>AC2</scene>, <scene name='pdbsite=AC3:Hcs+Binding+Site+For+Residue+A+802'>AC3</scene>, <scene name='pdbsite=AC4:Edo+Binding+Site+For+Residue+A+804'>AC4</scene>, <scene name='pdbsite=AC5:Hcs+Binding+Site+For+Residue+B+803'>AC5</scene> and <scene name='pdbsite=AC6:Edo+Binding+Site+For+Residue+B+805'>AC6</scene>
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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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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= <span class='plainlinks'>[http://en.wikipedia.org/wiki/5-methyltetrahydropteroyltriglutamate--homocysteine_S-methyltransferase 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.14 2.1.1.14] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= metE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 Thermotoga maritima])
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-->
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|DOMAIN=
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{{STRUCTURE_3bq5| PDB=3bq5 | SCENE= }}
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|RELATEDENTRY=[[1xdj|1XDJ]], [[3bof|3BOF]], [[3bol|3BOL]], [[3bq6|3BQ6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bq5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bq5 OCA], [http://www.ebi.ac.uk/pdbsum/3bq5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bq5 RCSB]</span>
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}}
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'''Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine (Monoclinic)'''
'''Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine (Monoclinic)'''
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[[Category: Pejchal, R.]]
[[Category: Pejchal, R.]]
[[Category: Smith, J L.]]
[[Category: Smith, J L.]]
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[[Category: amino-acid biosynthesis]]
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[[Category: Amino-acid biosynthesis]]
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[[Category: homocysteine]]
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[[Category: Homocysteine]]
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[[Category: metal-binding]]
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[[Category: Metal-binding]]
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[[Category: mete]]
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[[Category: Mete]]
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[[Category: methionine biosynthesis]]
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[[Category: Methionine biosynthesis]]
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[[Category: methyltransferase]]
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[[Category: Methyltransferase]]
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[[Category: tim barrel]]
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[[Category: Tim barrel]]
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[[Category: transferase]]
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[[Category: Transferase]]
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[[Category: zinc]]
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[[Category: Zinc]]
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[[Category: zinc inversion]]
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[[Category: Zinc inversion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 21:00:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:28:13 2008''
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Revision as of 18:00, 4 May 2008

Image:3bq5.jpg

Template:STRUCTURE 3bq5

Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ and Homocysteine (Monoclinic)


Overview

Enzymes possessing catalytic zinc centers perform a variety of fundamental processes in nature, including methyl transfer to thiols. Cobalamin-independent (MetE) and cobalamin-dependent (MetH) methionine synthases are two such enzyme families. Although they perform the same net reaction, transfer of a methyl group from methyltetrahydrofolate to homocysteine (Hcy) to form methionine, they display markedly different catalytic strategies, modular organization, and active site zinc centers. Here we report crystal structures of zinc-replete MetE and MetH, both in the presence and absence of Hcy. Structural investigation of the catalytic zinc sites of these two methyltransferases reveals an unexpected inversion of zinc geometry upon binding of Hcy and displacement of an endogenous ligand in both enzymes. In both cases a significant movement of the zinc relative to the protein scaffold accompanies inversion. These structures provide new information on the activation of thiols by zinc-containing enzymes and have led us to propose a paradigm for the mechanism of action of the catalytic zinc sites in these and related methyltransferases. Specifically, zinc is mobile in the active sites of MetE and MetH, and its dynamic nature helps facilitate the active site conformational changes necessary for thiol activation and methyl transfer.

About this Structure

3BQ5 is a Single protein structure of sequence from Thermotoga maritima. Full crystallographic information is available from OCA.

Reference

Metal active site elasticity linked to activation of homocysteine in methionine synthases., Koutmos M, Pejchal R, Bomer TM, Matthews RG, Smith JL, Ludwig ML, Proc Natl Acad Sci U S A. 2008 Mar 4;105(9):3286-91. Epub 2008 Feb 22. PMID:18296644 Page seeded by OCA on Sun May 4 21:00:05 2008

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