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| [[Image:1mmi.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1mmi| PDB=1mmi | SCENE= }} | | {{STRUCTURE_1mmi| PDB=1mmi | SCENE= }} |
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| '''E. COLI DNA POLYMERASE BETA SUBUNIT'''
| | ===E. COLI DNA POLYMERASE BETA SUBUNIT=== |
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| ==Overview==
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| The beta subunit of the Escherichia coli replicative DNA polymerase III holoenzyme is the sliding clamp that interacts with the alpha (polymerase) subunit to maintain the high processivity of the enzyme. The beta protein is a ring-shaped dimer of 40.6 kDa subunits whose structure has previously been determined at a resolution of 2.5 A [Kong et al. (1992), Cell, 69, 425-437]. Here, the construction of a new plasmid that directs overproduction of beta to very high levels and a simple procedure for large-scale purification of the protein are described. Crystals grown under slightly modified conditions diffracted to beyond 1.9 A at 100 K at a synchrotron source. The structure of the beta dimer solved at 1.85 A resolution shows some differences from that reported previously. In particular, it was possible at this resolution to identify residues that differed in position between the two subunits in the unit cell; side chains of these and some other residues were found to occupy alternate conformations. This suggests that these residues are likely to be relatively mobile in solution. Some implications of this flexibility for the function of beta are discussed. | | The line below this paragraph, {{ABSTRACT_PUBMED_12832762}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12832762 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12832762}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Processivity factor]] | | [[Category: Processivity factor]] |
| [[Category: Sliding clamp]] | | [[Category: Sliding clamp]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:25:15 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:22:46 2008'' |