3bol
From Proteopedia
(New page: 200px<br /><applet load="3bol" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bol, resolution 1.850Å" /> '''Cobalamin-dependent...) |
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| - | [[Image:3bol.jpg|left|200px]] | + | [[Image:3bol.jpg|left|200px]] |
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| - | '''Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima complexed with Zn2+''' | + | {{Structure |
| + | |PDB= 3bol |SIZE=350|CAPTION= <scene name='initialview01'>3bol</scene>, resolution 1.850Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Residue+A+701'>AC1</scene>, <scene name='pdbsite=AC2:Zn+Binding+Site+For+Residue+B+702'>AC2</scene>, <scene name='pdbsite=AC3:Zn+Binding+Site+For+Residue+B+703'>AC3</scene>, <scene name='pdbsite=AC4:K+Binding+Site+For+Residue+A+703'>AC4</scene>, <scene name='pdbsite=AC5:K+Binding+Site+For+Residue+B+704'>AC5</scene>, <scene name='pdbsite=AC6:Yt3+Binding+Site+For+Residue+A+705'>AC6</scene> and <scene name='pdbsite=AC7:Hcs+Binding+Site+For+Residue+B+710'>AC7</scene> | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=YT3:YTTRIUM+(III)+ION'>YT3</scene> and <scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC ACID'>HCS</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Methionine_synthase Methionine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.13 2.1.1.13] | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima complexed with Zn2+''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3BOL is a [ | + | 3BOL 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=3BOL OCA]. |
==Reference== | ==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:[http:// | + | 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: Methionine synthase]] | [[Category: Methionine synthase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc inversion]] | [[Category: zinc inversion]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 19:00:21 2008'' |
Revision as of 17:00, 20 March 2008
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| , resolution 1.850Å | |||||||
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| Sites: | , , , , , and | ||||||
| Ligands: | , , and | ||||||
| Activity: | Methionine synthase, with EC number 2.1.1.13 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Cobalamin-dependent methionine synthase (1-566) from Thermotoga maritima complexed with Zn2+
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
3BOL 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 Thu Mar 20 19:00:21 2008
Categories: Methionine synthase | Single protein | Thermotoga maritima | Koutmos, M. | Ludwig, M L. | Smith, J L. | HCS | K | YT3 | ZN | Meth | Methyltransferase | Tim barrel | Transferase | Zinc | Zinc inversion
