Motion in DNA Polymerase Beta (Pol Beta) [polbeta]

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Classification Known Domain Motion, Hinge Mechanism [D-h-2]

Structures
1BPD Conformation 1 [ PartsList ]
2BPF Conformation 2 [ PartsList ]
2BPG Conformation 3 [ PartsList ]

Description
Pol Beta contains 4 domains: 8-kD, F, P, and T. In both apo and ternary complexes the F, P, and T domains are arranged in such a way as to form a cleft for the DNA. In apo form the 8-kD domain, which is connected to the F domain, is moved away from the cleft. In the ternary complexes the 8-kD domain closes over the cleft to varying degrees through the motion of a singe flexible hinge of about 10 residues.

Particular values describing motion
Creation Date = 19970822
Modification Date = 19970822
Experimental Methods = x (Traditional x-ray)

References
M R Sawaya, H Pelletier, A Kumar, S H Wilson and J Kraut (1994). Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism. Science. 264: 1930-5. [Medline info for 94278498]

GO terms associated with structures
Molecular functionDNA binding, DNA-directed DNA polymerase activity, beta DNA polymerase activity
Cellular componentintracellular
Biological processDNA replication, DNA repair

Morphs

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Best representative
Morph Morph name Structure #1 Structure #2 Residues
DNA Polymerase beta 1bpd [ A ] 2bpg [ A ] 335

User-submitted morphs
Morph Morph name Structure #1 Structure #2 Residues
polbeta 1bpd [ ] 2bpf [ ] 335
605161-8387 DNA Polymerase Beta 1bpx [ A ] 1bpy [ A ] 335
817512-14947 polymerase beta 1bpx [ A ] 1bpy [ A ] 335
918240-24473 polymerase beta upload [ A ] upload [ B ] 326

Automatic morphs
Morph Morph name Structure #1 Structure #2 Residues
va1dk2A-1bnoA DNA Polymerase Beta 1dk2 [ A ] 1bno [ A ] 87
va1dk2A-1bnpA DNA Polymerase Beta 1dk2 [ A ] 1bnp [ A ] 87
va1dk3A-1bnpA DNA Polymerase Beta 1dk3 [ A ] 1bnp [ A ] 87
va1dk3A-1bnoA DNA Polymerase Beta 1dk3 [ A ] 1bno [ A ] 87
va1dk3A-1dk2A DNA Polymerase Beta 1dk3 [ A ] 1dk2 [ A ] 86

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Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu