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| - | [[Image:1xwl.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1xwl| PDB=1xwl | SCENE= }} | | {{STRUCTURE_1xwl| PDB=1xwl | SCENE= }} |
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| - | '''BACILLUS STEAROTHERMOPHILUS (NEWLY IDENTIFIED STRAIN AS YET UNNAMED) DNA POLYMERASE FRAGMENT'''
| + | ===BACILLUS STEAROTHERMOPHILUS (NEWLY IDENTIFIED STRAIN AS YET UNNAMED) DNA POLYMERASE FRAGMENT=== |
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| - | ==Overview==
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| - | BACKGROUND: The study of DNA polymerases in the Pol l family is central to the understanding of DNA replication and repair. DNA polymerases are used in many molecular biology techniques, including PCR, which require a thermostable polymerase. In order to learn about Pol I function and the basis of thermostability, we undertook structural studies of a new thermostable DNA polymerase. RESULTS: A DNA polymerase large, Klenow-like, fragment from a recently identified thermostable strain of Bacillus stearothermophilus (BF) was cloned, sequenced, overexpressed and characterized. Its crystal structure was determined to 2.1 A resolution by the method of multiple isomorphous replacement. CONCLUSIONS: This structure represents the highest resolution view of a Pol I enzyme obtained to date. Comparison of the three Pol I structures reveals no compelling evidence for many of the specific interactions that have been proposed to induce thermostability, but suggests that thermostability arises from innumerable small changes distributed throughout the protein structure. The polymerase domain is highly conserved in all three proteins. The N-terminal domains are highly divergent in sequence, but retain a common fold. When present, the 3'-5' proofreading exonuclease activity is associated with this domain. Its absence is associated with changes in catalytic residues that coordinate the divalent ions required for activity and in loops connecting homologous secondary structural elements. In BF, these changes result in a blockage of the DNA-binding cleft.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9016716}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9016716 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9016716}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Bf thermophilus polymerase]] | | [[Category: Bf thermophilus polymerase]] |
| | [[Category: Dna replication]] | | [[Category: Dna replication]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:35:50 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:47:37 2008'' |
Revision as of 20:47, 28 July 2008
Template:STRUCTURE 1xwl
BACILLUS STEAROTHERMOPHILUS (NEWLY IDENTIFIED STRAIN AS YET UNNAMED) DNA POLYMERASE FRAGMENT
Template:ABSTRACT PUBMED 9016716
About this Structure
1XWL is a Single protein structure of sequence from Geobacillus stearothermophilus. This structure supersedes the now removed PDB entry 1bdp. Full crystallographic information is available from OCA.
Reference
Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution., Kiefer JR, Mao C, Hansen CJ, Basehore SL, Hogrefe HH, Braman JC, Beese LS, Structure. 1997 Jan 15;5(1):95-108. PMID:9016716
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