2fll
From Proteopedia
Line 4: | Line 4: | ||
|PDB= 2fll |SIZE=350|CAPTION= <scene name='initialview01'>2fll</scene>, resolution 2.60Å | |PDB= 2fll |SIZE=350|CAPTION= <scene name='initialview01'>2fll</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
- | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | + | |LIGAND= <scene name='pdbligand=DA:2'-DEOXYADENOSINE-5'-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DOC:2',3'-DIDEOXYCYTIDINE-5'-MONOPHOSPHATE'>DOC</scene>, <scene name='pdbligand=DT:THYMIDINE-5'-MONOPHOSPHATE'>DT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=TTP:THYMIDINE-5'-TRIPHOSPHATE'>TTP</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= POLI, RAD30B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= POLI, RAD30B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY=[[1t3n|1T3N]], [[2azl|2AZL]], [[2fln|2FLN]], [[2flp|2FLP]] | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fll FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fll OCA], [http://www.ebi.ac.uk/pdbsum/2fll PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fll RCSB]</span> | ||
}} | }} | ||
Line 28: | Line 31: | ||
[[Category: Prakash, L.]] | [[Category: Prakash, L.]] | ||
[[Category: Prakash, S.]] | [[Category: Prakash, S.]] | ||
- | [[Category: MG]] | ||
- | [[Category: TTP]] | ||
[[Category: dna polymerase]] | [[Category: dna polymerase]] | ||
[[Category: lesion bypass]] | [[Category: lesion bypass]] | ||
Line 36: | Line 37: | ||
[[Category: y-family]] | [[Category: y-family]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:04:33 2008'' |
Revision as of 00:04, 31 March 2008
| |||||||
, resolution 2.60Å | |||||||
---|---|---|---|---|---|---|---|
Ligands: | , , , , , , | ||||||
Gene: | POLI, RAD30B (Homo sapiens) | ||||||
Activity: | DNA-directed DNA polymerase, with EC number 2.7.7.7 | ||||||
Related: | 1T3N, 2AZL, 2FLN, 2FLP
| ||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Ternary complex of human DNA polymerase iota with DNA and dTTP
Overview
Substrate-induced conformational change of the protein is the linchpin of enzymatic reactions. Replicative DNA polymerases, for example, convert from an open to a closed conformation in response to dNTP binding. Human DNA polymerase-iota (hPoliota), a member of the Y family of DNA polymerases, differs strikingly from other polymerases in its much higher proficiency and fidelity for nucleotide incorporation opposite template purines than opposite template pyrimidines. We present here a crystallographic analysis of hPoliota binary complexes, which together with the ternary complexes show that, contrary to replicative DNA polymerases, the DNA, and not the polymerase, undergoes the primary substrate-induced conformational change. The incoming dNTP "pushes" templates A and G from the anti to the syn conformation dictated by a rigid hPoliota active site. Together, the structures posit a mechanism for template selection wherein dNTP binding induces a conformational switch in template purines for productive Hoogsteen base pairing.
About this Structure
2FLL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
An incoming nucleotide imposes an anti to syn conformational change on the templating purine in the human DNA polymerase-iota active site., Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK, Structure. 2006 Apr;14(4):749-55. PMID:16615915
Page seeded by OCA on Mon Mar 31 03:04:33 2008