1ahc: Difference between revisions

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[[Image:1ahc.gif|left|200px]]


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==THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN==
The line below this paragraph, containing "STRUCTURE_1ahc", creates the "Structure Box" on the page.
<StructureSection load='1ahc' size='340' side='right'caption='[[1ahc]], [[Resolution|resolution]] 2.00&Aring;' 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'>[[1ahc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AHC FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</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&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ahc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ahc OCA], [https://pdbe.org/1ahc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ahc RCSB], [https://www.ebi.ac.uk/pdbsum/1ahc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ahc ProSAT]</span></td></tr>
{{STRUCTURE_1ahc| PDB=1ahc |  SCENE= }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/RIP1_MOMCH RIP1_MOMCH]
== 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/ah/1ahc_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=1ahc ConSurf].
<div style="clear:both"></div>


'''THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN'''
==See Also==
 
*[[Ribosome inactivating protein 3D structures|Ribosome inactivating protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
BACKGROUND: alpha-Momorcharin (alpha MMC) is a type I ribosome-inactivating protein. It inhibits protein synthesis by hydrolytically removing a specific adenine residue from a highly conserved, single-stranded loop of rRNA. RESULTS: Here we describe the determination and refinement of the crystal structures of alpha MMC in the native state and in complexes with the product, adenine, and a substrate analogue, formycin 5'-monophosphate (FMP) at high resolution. Both adenine and the base of FMP are tightly bound; the ribose of bound FMP adopts a strained, high-energy conformation, which may mimic the structure of the transition state. CONCLUSIONS: These structures indicate that residues Tyr70, Glu160 and Arg163 of alpha MMC are the most critical for catalysis. We propose that the strained conformation of the ribose in the target adenosine weakens the glycoside bond. Partial protonation mediated by Arg163 then facilitates N-glycoside bond cleavage, leading to the formation of an oxycarbonium ion intermediate which is stabilized by the negatively-charged Glu160. Tyr70 adopts subtly different conformations in the three structures implying that it may be important in substrate recognition and perhaps catalysis.
[[Category: Large Structures]]
 
==About this Structure==
1AHC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AHC OCA].
 
==Reference==
The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin., Ren J, Wang Y, Dong Y, Stuart DI, Structure. 1994 Jan 15;2(1):7-16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8075985 8075985]
[[Category: Momordica charantia]]
[[Category: Momordica charantia]]
[[Category: Single protein]]
[[Category: Dong Y]]
[[Category: RRNA N-glycosylase]]
[[Category: Ren J]]
[[Category: Dong, Y.]]
[[Category: Stuart DI]]
[[Category: Ren, J.]]
[[Category: Wang Y]]
[[Category: Stuart, D I.]]
[[Category: Wang, Y.]]
[[Category: Glycosidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:16:16 2008''

Latest revision as of 09:30, 7 February 2024

THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARINTHE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN

Structural highlights

1ahc is a 1 chain structure with sequence from Momordica charantia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RIP1_MOMCH

Evolutionary Conservation

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

See Also

1ahc, resolution 2.00Å

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