1z8s

From Proteopedia

(Difference between revisions)

Revision as of 16:58, 20 October 2021

DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)

Structural highlights

1z8s is a 1 chain structure with sequence from Atcc 12980. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	dnaG (ATCC 12980)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DNAG_GEOSE] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The helicase-primase interaction is a critical event in DNA replication and is mediated by a putative helicase-interaction domain within the primase. The solution structure of the helicase-interaction domain of DnaG reveals that it is made up of two independent subdomains: an N-terminal six-helix module and a C-terminal two-helix module that contains the residues of the primase previously identified as important in the interaction with the helicase. We show that the two-helix module alone is sufficient for strong binding between the primase and the helicase but fails to activate the helicase; both subdomains are required for helicase activation. The six-helix module of the primase has only one close structural homolog, the N-terminal domain of the corresponding helicase. This surprising structural relationship, coupled with the differences in surface properties of the two molecules, suggests how the helicase-interaction domain may perturb the structure of the helicase and lead to activation.

Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation.,Syson K, Thirlway J, Hounslow AM, Soultanas P, Waltho JP Structure. 2005 Apr;13(4):609-16. PMID:15837199^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Syson K, Thirlway J, Hounslow AM, Soultanas P, Waltho JP. Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. Structure. 2005 Apr;13(4):609-16. PMID:15837199 doi:10.1016/j.str.2005.01.022

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1z8s"

@@ Line 3: / Line 3: @@
 <StructureSection load='1z8s' size='340' side='right'caption='[[1z8s]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1z8s]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z8S OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Z8S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1z8s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_12980 Atcc 12980]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Z8S FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dnaG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1422 ATCC 12980])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1z8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z8s OCA], [http://pdbe.org/1z8s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1z8s RCSB], [http://www.ebi.ac.uk/pdbsum/1z8s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1z8s ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1z8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z8s OCA], [https://pdbe.org/1z8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1z8s RCSB], [https://www.ebi.ac.uk/pdbsum/1z8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1z8s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DNAG_GEOSE DNAG_GEOSE]] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]
+[[https://www.uniprot.org/uniprot/DNAG_GEOSE DNAG_GEOSE]] RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.[HAMAP-Rule:MF_00974]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1z8s

From Proteopedia

Revision as of 16:58, 20 October 2021

DnaB binding domain of DnaG (P16) from Bacillus stearothermophilus (residues 452-597)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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