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| - | [[Image:8adh.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_8adh| PDB=8adh | SCENE= }} | | {{STRUCTURE_8adh| PDB=8adh | SCENE= }} |
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| - | '''INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE BENDING MODE'''
| + | ===INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE BENDING MODE=== |
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| - | ==Overview==
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| - | A study of the hinge bending mode in the enzyme liver alcohol dehydrogenase is made by use of empirical energy functions. The enzyme is a dimer, with each monomer composed of a coenzyme binding domain and a catalytic domain with a large cleft between the two. Superposition of the apoenzyme and holoenzyme crystal structures is used to determine a rigid rotation axis for closing of the cleft. It is shown that a rigid body transformation of the apoenzyme to the holoenzyme structure corresponds to a 10 degrees rotation of the catalytic domain about this axis. The rotation is not along the least-motion path for closing of the cleft but instead corresponds to the catalytic domain coming closer to the coenzyme binding domain by a sliding motion. Estimation of the energy associated with the interdomain motion of the apoenzyme over a range of 90 degrees (-40 to 50 degrees, where 0 degrees corresponds to the minimized crystal structure) demonstrates that local structural relaxation makes possible large-scale rotations with relatively small energy increments. A variety of structural rearrangements associated with the domain motion are characterized. They involve the hinge region residues that provide the covalent connections between the two domains and certain loop regions that are brought into contact by the rotation. Differences between the energy minimized and the holoenzyme structures point to the existence of alternative conformations for loops and to the importance of the ligands in the structural rearrangements.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_3771574}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 3771574 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_3771574}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Eklund, H.]] | | [[Category: Eklund, H.]] |
| | [[Category: Jones, T A.]] | | [[Category: Jones, T A.]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:48:30 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Jul 11 12:53:02 2008'' |
Revision as of 09:53, 11 July 2008
Template:STRUCTURE 8adh
INTERDOMAIN MOTION IN LIVER ALCOHOL DEHYDROGENASE. STRUCTURAL AND ENERGETIC ANALYSIS OF THE HINGE BENDING MODE
Template:ABSTRACT PUBMED 3771574
About this Structure
8ADH is a Single protein structure of sequence from Equus caballus. This structure supersedes the now removed PDB entries and 3adh. Full crystallographic information is available from OCA.
Reference
Interdomain motion in liver alcohol dehydrogenase. Structural and energetic analysis of the hinge bending mode., Colonna-Cesari F, Perahia D, Karplus M, Eklund H, Braden CI, Tapia O, J Biol Chem. 1986 Nov 15;261(32):15273-80. PMID:3771574
Page seeded by OCA on Fri Jul 11 12:53:02 2008
