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| - | [[Image:1kol.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1kol.png|left|200px]] |
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| | {{STRUCTURE_1kol| PDB=1kol | SCENE= }} | | {{STRUCTURE_1kol| PDB=1kol | SCENE= }} |
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| - | '''Crystal structure of formaldehyde dehydrogenase'''
| + | ===Crystal structure of formaldehyde dehydrogenase=== |
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| - | ==Overview==
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| - | Formaldehyde dehydrogenase from Pseudomonas putida (PFDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase family. The pyridine nucleotide NAD(H) in PFDH, which is distinct from the coenzyme (as cosubstrate) in typical alcohol dehydrogenases (ADHs), is tightly but not covalently bound to the protein and acts as a cofactor. PFDH can catalyze aldehyde dismutations without an external addition of NAD(H). The structural basis of the tightly bound cofactor of PFDH is unknown. The crystal structure of PFDH has been solved by the multiwavelength anomalous diffraction method using intrinsic zinc ions and has been refined at a 1.65 A resolution. The 170-kDa homotetrameric PFDH molecule shows 222 point group symmetry. Although the secondary structure arrangement and the binding mode of catalytic and structural zinc ions in PFDH are similar to those of typical ADHs, a number of loop structures that differ between PFDH and ADHs in their lengths and conformations are observed. A comparison of the present structure of PFDH with that of horse liver ADH, a typical example of an ADH, reveals that a long insertion loop of PFDH shields the adenine part of the bound NAD(+) molecule from the solvent, and a tight hydrogen bond network exists between the insertion loop and the adenine part of the cofactor, which is unique to PFDH. This insertion loop is conserved completely among the aldehyde-dismutating formaldehyde dehydrogenases, whereas it is replaced by a short turn among typical ADHs. Thus, the insertion loop specifically found among the aldehyde-dismutating formaldehyde dehydrogenases is responsible for the tight cofactor binding of these enzymes and explains why PFDH can effectively catalyze alternate oxidation and reduction of aldehydes without the release of cofactor molecule from the enzyme.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12445786}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12445786 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12445786}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Yoshimoto, T.]] | | [[Category: Yoshimoto, T.]] |
| | [[Category: Dehydrogenase]] | | [[Category: Dehydrogenase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:59:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:39:48 2008'' |
Revision as of 07:39, 2 July 2008
Template:STRUCTURE 1kol
Crystal structure of formaldehyde dehydrogenase
Template:ABSTRACT PUBMED 12445786
About this Structure
1KOL is a Single protein structure of sequence from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of formaldehyde dehydrogenase from Pseudomonas putida: the structural origin of the tightly bound cofactor in nicotinoprotein dehydrogenases., Tanaka N, Kusakabe Y, Ito K, Yoshimoto T, Nakamura KT, J Mol Biol. 2002 Nov 29;324(3):519-33. PMID:12445786
Page seeded by OCA on Wed Jul 2 10:39:48 2008
