1bpd

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[[Image:1bpd.gif|left|200px]]
[[Image:1bpd.gif|left|200px]]
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{{Structure
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|PDB= 1bpd |SIZE=350|CAPTION= <scene name='initialview01'>1bpd</scene>, resolution 3.60&Aring;
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The line below this paragraph, containing "STRUCTURE_1bpd", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] </span>
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{{STRUCTURE_1bpd| PDB=1bpd | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bpd OCA], [http://www.ebi.ac.uk/pdbsum/1bpd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bpd RCSB]</span>
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'''CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM'''
'''CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM'''
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[[Category: Sawaya, M R.]]
[[Category: Sawaya, M R.]]
[[Category: Wilson, S H.]]
[[Category: Wilson, S H.]]
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[[Category: nucleotidyltransferase]]
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[[Category: Nucleotidyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:47:49 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:05:33 2008''
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Revision as of 08:47, 2 May 2008

Template:STRUCTURE 1bpd

CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM


Overview

Structures of the 31-kilodalton catalytic domain of rat DNA polymerase beta (pol beta) and the whole 39-kilodalton enzyme were determined at 2.3 and 3.6 angstrom resolution, respectively. The 31-kilodalton domain is composed of fingers, palm, and thumb subdomains arranged to form a DNA binding channel reminiscent of the polymerase domains of the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, and bacteriophage T7 RNA polymerase. The amino-terminal 8-kilodalton domain is attached to the fingers subdomain by a flexible hinge. The two invariant aspartates found in all polymerase sequences and implicated in catalytic activity have the same geometric arrangement within structurally similar but topologically distinct palms, indicating that the polymerases have maintained, or possibly re-evolved, a common nucleotidyl transfer mechanism. The location of Mn2+ and deoxyadenosine triphosphate in pol beta confirms the role of the invariant aspartates in metal ion and deoxynucleoside triphosphate binding.

About this Structure

1BPD is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism., Sawaya MR, Pelletier H, Kumar A, Wilson SH, Kraut J, Science. 1994 Jun 24;264(5167):1930-5. PMID:7516581 Page seeded by OCA on Fri May 2 11:47:49 2008

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