3bq6

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(New page: 200px<br /><applet load="3bq6" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bq6, resolution 2.1&Aring;" /> '''Crystal Structure of ...)
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[[Image:3bq6.jpg|left|200px]]<br /><applet load="3bq6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:3bq6.jpg|left|200px]]
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caption="3bq6, resolution 2.1&Aring;" />
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'''Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ (Monoclinic)'''<br />
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{{Structure
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|PDB= 3bq6 |SIZE=350|CAPTION= <scene name='initialview01'>3bq6</scene>, resolution 2.1&Aring;
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|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+800'>AC1</scene> and <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+801'>AC2</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
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|ACTIVITY= [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]
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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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'''Crystal Structure of T. maritima Cobalamin-Independent Methionine Synthase complexed with Zn2+ (Monoclinic)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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3BQ6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Known structural/functional Sites: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+800'>AC1</scene> and <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+801'>AC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BQ6 OCA].
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3BQ6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BQ6 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18296644 18296644]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/18296644 18296644]
[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
[[Category: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc inversion]]
[[Category: zinc inversion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Mar 14 09:39:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:00:36 2008''

Revision as of 17:00, 20 March 2008

Image:3bq6.jpg


PDB ID 3bq6

Drag the structure with the mouse to rotate
, resolution 2.1Å
Sites: and
Ligands:
Gene: metE (Thermotoga maritima)
Activity: 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase, with EC number 2.1.1.14
Coordinates: save as pdb, mmCIF, xml



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

3BQ6 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

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