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New page: left|200px<br /> <applet load="1d8v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d8v" /> '''THE RESTRAINED AND MINIMIZED AVERAGE NMR ST...
 
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[[Image:1d8v.gif|left|200px]]<br />
<applet load="1d8v" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1d8v" />
'''THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.'''<br />


==Overview==
==THE RESTRAINED AND MINIMIZED AVERAGE NMR STRUCTURE OF MAP30.==
We present the solution structure of MAP30, a plant protein with anti-HIV, and anti-tumor activities. Structural analysis and subsequent biochemical, assays lead to several novel discoveries. First, MAP30 acts like a DNA, glycosylase/apurinic (ap) lyase, an additional activity distinct from its, known RNA N-glycosidase activity toward the 28S rRNA. Glycosylase/ap lyase, activity explains MAP30's apparent inhibition of the HIV-1 integrase, MAP30's ability to irreversibly relax supercoiled DNA, and may be an, alternative cytotoxic pathway that contributes to MAP30's, anti-HIV/anti-tumor activities. Second, two distinct, but contiguous, subsites are responsible for MAP30's glycosylase/ap lyase activity. Third, Mn2+ and Zn2+ interact with negatively charged surfaces next to the, catalytic sites, facilitating DNA substrate binding instead of directly, participating in catalysis.
<StructureSection load='1d8v' size='340' side='right'caption='[[1d8v]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1d8v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D8V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1d8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d8v OCA], [https://pdbe.org/1d8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d8v RCSB], [https://www.ebi.ac.uk/pdbsum/1d8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d8v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RIP3_MOMCH RIP3_MOMCH] Irreversibly relaxes supercoiled DNA and catalyzes double-stranded breakage. Acts also as a ribosome inactivating protein.
== 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/d8/1d8v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1d8v ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We present the solution structure of MAP30, a plant protein with anti-HIV and anti-tumor activities. Structural analysis and subsequent biochemical assays lead to several novel discoveries. First, MAP30 acts like a DNA glycosylase/apurinic (ap) lyase, an additional activity distinct from its known RNA N-glycosidase activity toward the 28S rRNA. Glycosylase/ap lyase activity explains MAP30's apparent inhibition of the HIV-1 integrase, MAP30's ability to irreversibly relax supercoiled DNA, and may be an alternative cytotoxic pathway that contributes to MAP30's anti-HIV/anti-tumor activities. Second, two distinct, but contiguous, subsites are responsible for MAP30's glycosylase/ap lyase activity. Third, Mn2+ and Zn2+ interact with negatively charged surfaces next to the catalytic sites, facilitating DNA substrate binding instead of directly participating in catalysis.


==About this Structure==
Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions.,Wang YX, Neamati N, Jacob J, Palmer I, Stahl SJ, Kaufman JD, Huang PL, Huang PL, Winslow HE, Pommier Y, Wingfield PT, Lee-Huang S, Bax A, Torchia DA Cell. 1999 Nov 12;99(4):433-42. PMID:10571185<ref>PMID:10571185</ref>
1D8V is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D8V OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural insights into its multiple functions., Wang YX, Neamati N, Jacob J, Palmer I, Stahl SJ, Kaufman JD, Huang PL, Huang PL, Winslow HE, Pommier Y, Wingfield PT, Lee-Huang S, Bax A, Torchia DA, Cell. 1999 Nov 12;99(4):433-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10571185 10571185]
</div>
<div class="pdbe-citations 1d8v" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Momordica charantia]]
[[Category: Momordica charantia]]
[[Category: Single protein]]
[[Category: Jacob J]]
[[Category: Jacob, J.]]
[[Category: Neamati N]]
[[Category: Neamati, N.]]
[[Category: Palmer I]]
[[Category: Palmer, I.]]
[[Category: Stahl SJ]]
[[Category: Stahl, S.J.]]
[[Category: Wang Y-X]]
[[Category: Wang, Y.X.]]
[[Category: single chain]]
 
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