1xwl

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[[Image:1xwl.gif|left|200px]]<br /><applet load="1xwl" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1xwl.gif|left|200px]]
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caption="1xwl, resolution 1.70&Aring;" />
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'''BACILLUS STEAROTHERMOPHILUS (NEWLY IDENTIFIED STRAIN AS YET UNNAMED) DNA POLYMERASE FRAGMENT'''<br />
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{{Structure
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|PDB= 1xwl |SIZE=350|CAPTION= <scene name='initialview01'>1xwl</scene>, resolution 1.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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|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]
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|GENE= BACILLUS STEAROTHERMOPHILUS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 Geobacillus stearothermophilus])
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}}
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'''BACILLUS STEAROTHERMOPHILUS (NEWLY IDENTIFIED STRAIN AS YET UNNAMED) DNA POLYMERASE FRAGMENT'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1XWL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. This structure supersedes the now removed PDB entry 1BDP. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWL OCA].
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1XWL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus]. This structure supersedes the now removed PDB entry 1BDP. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWL OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9016716 9016716]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9016716 9016716]
[[Category: DNA-directed DNA polymerase]]
[[Category: DNA-directed DNA polymerase]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
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[[Category: dna replication]]
[[Category: dna replication]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:15:26 2008''

Revision as of 13:15, 20 March 2008


PDB ID 1xwl

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands:
Gene: BACILLUS STEAROTHERMOPHILUS (Geobacillus stearothermophilus)
Activity: DNA-directed DNA polymerase, with EC number 2.7.7.7
Coordinates: save as pdb, mmCIF, xml



BACILLUS STEAROTHERMOPHILUS (NEWLY IDENTIFIED STRAIN AS YET UNNAMED) DNA POLYMERASE FRAGMENT


Overview

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.

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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