1mc5
From Proteopedia
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| - | [[Image:1mc5.gif|left|200px]] | + | [[Image:1mc5.gif|left|200px]] |
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| - | '''Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with S-(hydroxymethyl)glutathione and NADH''' | + | {{Structure |
| + | |PDB= 1mc5 |SIZE=350|CAPTION= <scene name='initialview01'>1mc5</scene>, resolution 2.60Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene> and <scene name='pdbligand=AHE:2-AMINO-4-[1-CARBOXYMETHYL-CARBAMOYL)-2-HYDROXYMETHYLSULFANYL-ETHYLCARBAMOYL]-BUTYRIC ACID'>AHE</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= ADH5 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | }} | ||
| + | |||
| + | '''Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with S-(hydroxymethyl)glutathione and NADH''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MC5 is a [ | + | 1MC5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MC5 OCA]. |
==Reference== | ==Reference== | ||
| - | Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation., Sanghani PC, Bosron WF, Hurley TD, Biochemistry. 2002 Dec 24;41(51):15189-94. PMID:[http:// | + | Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation., Sanghani PC, Bosron WF, Hurley TD, Biochemistry. 2002 Dec 24;41(51):15189-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12484756 12484756] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: s-(hydroxymethyl)glutathione]] | [[Category: s-(hydroxymethyl)glutathione]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:41:38 2008'' |
Revision as of 10:41, 20 March 2008
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| , resolution 2.60Å | |||||||
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| Ligands: | , , , and | ||||||
| Gene: | ADH5 (Homo sapiens) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with S-(hydroxymethyl)glutathione and NADH
Overview
Human glutathione-dependent formaldehyde dehydrogenase plays an important role in the metabolism of glutathione adducts such as S-(hydroxymethyl)glutathione and S-nitrosoglutathione. The role of specific active site residues in binding these physiologically important substrates and the structural changes during the catalytic cycle of glutathione-dependent formaldehyde dehydrogenase was examined by determining the crystal structure of a ternary complex with S-(hydroxymethyl)glutathione and the reduced coenzyme to 2.6 A resolution. The formation of the ternary complex caused the movement of the catalytic domain toward the coenzyme-binding domain. This represents the first observation of domain closure in glutathione-dependent formaldehyde dehydrogenase in response to substrate binding. A water molecule adjacent to the 2'-ribose hydroxyl of NADH suggests that the alcohol proton is relayed to solvent directly from the coenzyme, rather than through the action of the terminal histidine residue as observed in the proton relay system for class I alcohol dehydrogenases. S-(Hydroxymethyl)glutathione is directly coordinated to the active site zinc and forms interactions with the highly conserved residues Arg114, Asp55, Glu57, and Thr46. The active site zinc has a tetrahedral coordination environment with Cys44, His66, and Cys173 as the three protein ligands in addition to S-(hydroxymethyl)glutathione. This is in contrast to zinc coordination in the binary coenzyme complex where all of the ligands were contributed by the enzyme and included Glu67 as the fourth protein ligand. This change in zinc coordination is accomplished by an approximately 2.3 A movement of the catalytic zinc.
About this Structure
1MC5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation., Sanghani PC, Bosron WF, Hurley TD, Biochemistry. 2002 Dec 24;41(51):15189-94. PMID:12484756
Page seeded by OCA on Thu Mar 20 12:41:38 2008
