From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1mc5.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1mc5.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1mc5| PDB=1mc5 | SCENE= }} | | {{STRUCTURE_1mc5| PDB=1mc5 | SCENE= }} |
| | | | |
| - | '''Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with S-(hydroxymethyl)glutathione and NADH'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12484756}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12484756 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12484756}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 27: |
Line 31: |
| | [[Category: Class iii alcohol dehydrogenase]] | | [[Category: Class iii alcohol dehydrogenase]] |
| | [[Category: Glutathione-dependent formaldehyde dehydrogenase]] | | [[Category: Glutathione-dependent formaldehyde dehydrogenase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:52:48 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:39:48 2008'' |
Revision as of 20:39, 2 July 2008
Template:STRUCTURE 1mc5
Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with S-(hydroxymethyl)glutathione and NADH
Template:ABSTRACT PUBMED 12484756
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 Wed Jul 2 23:39:48 2008
