1i1v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (10:56, 4 August 2021) (edit) (undo)
 
(8 intermediate revisions not shown.)
Line 1: Line 1:
{{Theoretical_model}}
{{Theoretical_model}}
-
{{Seed}}
 
-
[[Image:1i1v.png|left|200px]]
 
-
<!--
+
==A THEORETICAL MODEL OF TRIPLE-STRANDED DNA BOUND TO RECA PROTEIN (N-S INTERCONVERSION MODEL)==
-
The line below this paragraph, containing "STRUCTURE_1i1v", creates the "Structure Box" on the page.
+
<StructureSection load='1i1v' size='340' side='right'caption='[[1i1v]]' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I1V FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</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=1i1v FirstGlance], [https://www.ebi.ac.uk/pdbsum/1i1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i1v ProSAT]</span></td></tr>
-
-->
+
</table>
-
{{STRUCTURE_1i1v| PDB=1i1v | SCENE= }}
+
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Escherichia coli RecA is a representative of proteins from the RecA family, which promote homologous pairing and strand exchange between double-stranded DNA and single-stranded DNA. These reactions are essential for homologous genetic recombination in various organisms. From NMR studies, we previously reported a novel deoxyribose-base stacking interaction between adjacent residues on the extended single-stranded DNA bound to RecA protein. In this study, we found that the same DNA structure was induced by the binding to Saccharomyces cerevisiae Rad51 protein, indicating that the unique DNA structure induced by the binding to RecA-homologs was conserved from prokaryotes to eukaryotes. On the basis of this structure, we have formulated the structure of duplex DNA within filaments formed by RecA protein and its homologs. Two types of molecular structures are presented. One is the duplex structure that has the N-type sugar pucker. Its helical pitch is approximately 95 A (18.6 bp/turn), corresponding to that of an active, or ATP-form of the RecA filament. The other is one that has the S-type sugar pucker. Its helical pitch is approximately 64 A (12.5 bp/turn), corresponding to that of an inactive, or ADP-form of the RecA filament. During this modeling, we found that the interconversion of sugar puckers between the N-type and the S-type rotates bases horizontally, while maintaining the deoxyribose-base stacking interaction. We propose that this base rotation enables base pair switching between double-stranded DNA and single-stranded DNA to take place, facilitating homologous pairing and strand exchange. A possible mechanism for strand exchange involving DNA rotation also is discussed.
-
===A THEORETICAL MODEL OF TRIPLE-STRANDED DNA BOUND TO RECA PROTEIN (N-S INTERCONVERSION MODEL)===
+
Base pair switching by interconversion of sugar puckers in DNA extended by proteins of RecA-family: a model for homology search in homologous genetic recombination.,Nishinaka T, Shinohara A, Ito Y, Yokoyama S, Shibata T Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11071-6. PMID:9736691<ref>PMID:9736691</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_9736691}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1i1v" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 9736691 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_9736691}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Theoretical Model]]
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1V OCA].
+
[[Category: Large Structures]]
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:9736691</ref><references group="xtra"/>
+
[[Category: Ito, Y]]
[[Category: Ito, Y]]
[[Category: Nishinaka, T]]
[[Category: Nishinaka, T]]
Line 30: Line 27:
[[Category: Shinohara, A]]
[[Category: Shinohara, A]]
[[Category: Yokoyama, S]]
[[Category: Yokoyama, S]]
- 
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 06:48:46 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

A THEORETICAL MODEL OF TRIPLE-STRANDED DNA BOUND TO RECA PROTEIN (N-S INTERCONVERSION MODEL)

PDB ID 1i1v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i1v"
Personal tools