2ido: Difference between revisions

Revision as of 18:51, 21 February 2008

Structure of the E. coli Pol III epsilon-Hot proofreading complex

OverviewOverview

The epsilon subunit of Escherichia coli DNA polymerase III possesses 3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon is tightly bound between the alpha subunit (DNA polymerase) and subunit. Here, we present the crystal structure of epsilon in complex with HOT, the bacteriophage P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT interface is defined by two areas of contact: an interaction of the previously unstructured N terminus of HOT with an edge of the epsilon central beta-sheet as well as interactions between HOT and the catalytically important helix alpha1-loop-helix alpha2 motif of epsilon. This structure provides insight into how HOT and, by implication, may stabilize the epsilon subunit, thus promoting efficient proofreading during chromosomal replication.

About this StructureAbout this Structure

2IDO is a Protein complex structure of sequences from Enterobacteria phage p21 and Escherichia coli with , and as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

ReferenceReference

Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex., Kirby TW, Harvey S, DeRose EF, Chalov S, Chikova AK, Perrino FW, Schaaper RM, London RE, Pedersen LC, J Biol Chem. 2006 Dec 15;281(50):38466-71. Epub 2006 Sep 13. PMID:16973612

Page seeded by OCA on Thu Feb 21 17:51:38 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ido.gif|left|200px]]<br /><applet load="2ido" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2ido.gif|left|200px]]<br /><applet load="2ido" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2ido, resolution 2.10&Aring;" />
 '''Structure of the E. coli Pol III epsilon-Hot proofreading complex'''<br />
 ==Overview==
-The epsilon subunit of Escherichia coli DNA polymerase III possesses, 3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon, is tightly bound between the alpha subunit (DNA polymerase) and subunit., Here, we present the crystal structure of epsilon in complex with HOT, the, bacteriophage P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT, interface is defined by two areas of contact: an interaction of the, previously unstructured N terminus of HOT with an edge of the epsilon, central beta-sheet as well as interactions between HOT and the, catalytically important helix alpha1-loop-helix alpha2 motif of epsilon., This structure provides insight into how HOT and, by implication, may, stabilize the epsilon subunit, thus promoting efficient proofreading, during chromosomal replication.
+The epsilon subunit of Escherichia coli DNA polymerase III possesses 3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon is tightly bound between the alpha subunit (DNA polymerase) and subunit. Here, we present the crystal structure of epsilon in complex with HOT, the bacteriophage P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT interface is defined by two areas of contact: an interaction of the previously unstructured N terminus of HOT with an edge of the epsilon central beta-sheet as well as interactions between HOT and the catalytically important helix alpha1-loop-helix alpha2 motif of epsilon. This structure provides insight into how HOT and, by implication, may stabilize the epsilon subunit, thus promoting efficient proofreading during chromosomal replication.
 ==About this Structure==
-IDO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, TMP and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IDO OCA].
+IDO is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21] and [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=TMP:'>TMP</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2IDO OCA].
 ==Reference==
@@ Line 16: / Line 16: @@
 [[Category: Protein complex]]
 [[Category: Chalov, S.]]
-[[Category: Chikova, A.K.]]
+[[Category: Chikova, A K.]]
-[[Category: DeRose, E.F.]]
+[[Category: DeRose, E F.]]
 [[Category: Harvey, S.]]
-[[Category: Kirby, T.W.]]
+[[Category: Kirby, T W.]]
-[[Category: London, R.E.]]
+[[Category: London, R E.]]
-[[Category: Pedersen, L.C.]]
+[[Category: Pedersen, L C.]]
-[[Category: Perrino, F.W.]]
+[[Category: Perrino, F W.]]
-[[Category: Schaaper, R.M.]]
+[[Category: Schaaper, R M.]]
 [[Category: EDO]]
 [[Category: MN]]
@@ Line 33: / Line 33: @@
 [[Category: polymerase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:15:39 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:51:38 2008''