2fmq: Difference between revisions

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|PDB= 2fmq |SIZE=350|CAPTION= <scene name='initialview01'>2fmq</scene>, resolution 2.20&Aring;
|PDB= 2fmq |SIZE=350|CAPTION= <scene name='initialview01'>2fmq</scene>, resolution 2.20&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=DUP:2&#39;-DEOXYURIDINE 5&#39;-ALPHA,BETA-IMIDO-TRIPHOSPHATE'>DUP</scene>
|LIGAND= <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=DUP:2&#39;-DEOXYURIDINE+5&#39;-ALPHA,BETA-IMIDO-TRIPHOSPHATE'>DUP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>
|ACTIVITY= [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]  
|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>
|GENE= POLB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|GENE= POLB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
|DOMAIN=
|RELATEDENTRY=[[2fmp|2FMP]], [[2fms|2FMS]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fmq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fmq OCA], [http://www.ebi.ac.uk/pdbsum/2fmq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fmq RCSB]</span>
}}
}}


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[[Category: Shock, D D.]]
[[Category: Shock, D D.]]
[[Category: Wilson, S H.]]
[[Category: Wilson, S H.]]
[[Category: DUP]]
[[Category: MG]]
[[Category: NA]]
[[Category: nucleotidyl transferase]]
[[Category: nucleotidyl transferase]]


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Revision as of 00:04, 31 March 2008

File:2fmq.gif


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2fmq, resolution 2.20Å
Ligands: DA, DC, DG, DT, DUP, MG, NA
Gene: POLB (Homo sapiens)
Activity: DNA-directed DNA polymerase, with EC number 2.7.7.7
Related: 2FMP, 2FMS


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Sodium in active site of DNA Polymerase Beta


Overview

The molecular details of the nucleotidyl transferase reaction have remained speculative, as strategies to trap catalytic intermediates for structure determination utilize substrates lacking the primer terminus 3'-OH and catalytic Mg2+, resulting in an incomplete and distorted active site geometry. Since the geometric arrangement of these essential atoms will impact chemistry, structural insight into fidelity strategies has been hampered. Here, we present a crystal structure of a precatalytic complex of a DNA polymerase with bound substrates that include the primer 3'-OH and catalytic Mg2+. This catalytic intermediate was trapped with a nonhydrolyzable deoxynucleotide analog. Comparison with two new structures of DNA polymerase beta lacking the 3'-OH or catalytic Mg2+ is described. These structures provide direct evidence that both atoms are required to achieve a proper geometry necessary for an in-line nucleophilic attack of O3' on the alphaP of the incoming nucleotide.

About this Structure

2FMQ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Magnesium-induced assembly of a complete DNA polymerase catalytic complex., Batra VK, Beard WA, Shock DD, Krahn JM, Pedersen LC, Wilson SH, Structure. 2006 Apr;14(4):757-66. PMID:16615916

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