1v1q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (00:35, 21 November 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1v1q.gif|left|200px]]<br />
 
-
<applet load="1v1q" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1v1q, resolution 2.10&Aring;" />
 
-
'''CRYSTAL STRUCTURE OF PRIB- A PRIMOSOMAL DNA REPLICATION PROTEIN OF ESCHERICHIA COLI'''<br />
 
-
==Overview==
+
==Crystal structure of PriB- a primosomal DNA replication protein of Escherichia coli==
-
PriB is one of the Escherichia coli varphiX-type primosome proteins that, are required for assembly of the primosome, a mobile multi-enzyme complex, responsible for the initiation of DNA replication. Here we report the, crystal structure of the E. coli PriB at 2.1 A resolution by, multi-wavelength anomalous diffraction using a mercury derivative. The, polypeptide chain of PriB is structurally similar to that of, single-stranded DNA-binding protein (SSB). However, the biological unit of, PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility, shift assays demonstrated that PriB binds single-stranded DNA and, single-stranded RNA with comparable affinity. We also show that PriB binds, single-stranded DNA with certain base preferences. Based on the PriB, structural information and biochemical studies, we propose that the, potential tetramer formation surface and several other regions of PriB may, participate in protein-protein interaction during DNA replication. These, findings may illuminate the role of PriB in varphiX-type primosome, assembly.
+
<StructureSection load='1v1q' size='340' side='right'caption='[[1v1q]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1v1q]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V1Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V1Q FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYS:CYSTEINE'>CYS</scene></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=1v1q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v1q OCA], [https://pdbe.org/1v1q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v1q RCSB], [https://www.ebi.ac.uk/pdbsum/1v1q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v1q ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/PRIB_ECOLI PRIB_ECOLI] Binds single-stranded DNA at the primosome assembly site (PAS). During primosome assembly it facilitates the complex formation between PriA and DnaT.<ref>PMID:1856227</ref> <ref>PMID:1646811</ref> <ref>PMID:8366072</ref>
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v1/1v1q_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1v1q ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
PriB is one of the Escherichia coli varphiX-type primosome proteins that are required for assembly of the primosome, a mobile multi-enzyme complex responsible for the initiation of DNA replication. Here we report the crystal structure of the E. coli PriB at 2.1 A resolution by multi-wavelength anomalous diffraction using a mercury derivative. The polypeptide chain of PriB is structurally similar to that of single-stranded DNA-binding protein (SSB). However, the biological unit of PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility shift assays demonstrated that PriB binds single-stranded DNA and single-stranded RNA with comparable affinity. We also show that PriB binds single-stranded DNA with certain base preferences. Based on the PriB structural information and biochemical studies, we propose that the potential tetramer formation surface and several other regions of PriB may participate in protein-protein interaction during DNA replication. These findings may illuminate the role of PriB in varphiX-type primosome assembly.
-
==About this Structure==
+
Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli.,Liu JH, Chang TW, Huang CY, Chen SU, Wu HN, Chang MC, Hsiao CD J Biol Chem. 2004 Nov 26;279(48):50465-71. Epub 2004 Sep 21. PMID:15383524<ref>PMID:15383524</ref>
-
1V1Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CYS and CYS as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V1Q OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Crystal structure of PriB, a primosomal DNA replication protein of Escherichia coli., Liu JH, Chang TW, Huang CY, Chen SU, Wu HN, Chang MC, Hsiao CD, J Biol Chem. 2004 Nov 26;279(48):50465-71. Epub 2004 Sep 21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15383524 15383524]
+
</div>
-
[[Category: Escherichia coli]]
+
<div class="pdbe-citations 1v1q" style="background-color:#fffaf0;"></div>
-
[[Category: Single protein]]
+
== References ==
-
[[Category: Chang, M.C.]]
+
<references/>
-
[[Category: Chang, T.W.]]
+
__TOC__
-
[[Category: Chen, S.U.]]
+
</StructureSection>
-
[[Category: Hsiao, C.D.]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: Huang, C.Y.]]
+
[[Category: Large Structures]]
-
[[Category: Liu, J.H.]]
+
[[Category: Chang M-C]]
-
[[Category: Wu, H.N.]]
+
[[Category: Chang T-W]]
-
[[Category: CYS]]
+
[[Category: Chen S-U]]
-
[[Category: dna binding]]
+
[[Category: Hsiao C-D]]
-
[[Category: dna replication]]
+
[[Category: Huang C-Y]]
-
[[Category: primosome]]
+
[[Category: Liu J-H]]
-
 
+
[[Category: Wu H-N]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 17:18:58 2007''
+

Current revision

Crystal structure of PriB- a primosomal DNA replication protein of Escherichia coli

PDB ID 1v1q

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools