1bk7

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(New page: 200px<br /><applet load="1bk7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bk7, resolution 1.75&Aring;" /> '''RIBONUCLEASE MC1 FRO...)
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[[Image:1bk7.jpg|left|200px]]<br /><applet load="1bk7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bk7, resolution 1.75&Aring;" />
 
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'''RIBONUCLEASE MC1 FROM THE SEEDS OF BITTER GOURD'''<br />
 
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==Overview==
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==RIBONUCLEASE MC1 FROM THE SEEDS OF BITTER GOURD==
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The ribonuclease MC1 (RNase MC1) from seeds of bitter gourd (Momordica, charantia) consists of 190 amino acid residues with four disulfide bridges, and belongs to the RNase T(2) family, including fungal RNases typified by, RNase Rh from Rhizopus niveus and RNase T(2) from Aspergillus oryzae. The, crystal structure of RNase MC1 has been determined at 1.75 A resolution, with an R-factor of 19.7% using the single isomorphous replacement method., RNase MC1 structurally belongs to the (alpha+beta) class of proteins, having ten helices (six alpha-helices and four 3(10)-helices) and eight, beta-strands. When the structures of RNase MC1 and RNase Rh are, superposed, the close agreement between the alpha-carbon positions for the, total structure is obvious: the root mean square deviations calculated, only for structurally related 151 alpha-carbon atoms of RNase MC1 and, RNase Rh molecules was 1.76 A. Furthermore, the conformation of the, catalytic residues His-46, Glu-105, and His-109 in RNase Rh can be easily, superposed with that of the possible catalytic residues His-34, Glu-84, and His-88 in RNase MC1. This observation strongly indicates that RNase, MC1 from a plant origin catalyzes RNA degradation in a similar manner as, fungal RNases.
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<StructureSection load='1bk7' size='340' side='right'caption='[[1bk7]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bk7]] 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=1BK7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BK7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#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=1bk7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bk7 OCA], [https://pdbe.org/1bk7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bk7 RCSB], [https://www.ebi.ac.uk/pdbsum/1bk7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bk7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RNMC1_MOMCH RNMC1_MOMCH] Ribonuclease cleaving preferentially the 5'-side of uridine.<ref>PMID:10964705</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bk/1bk7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1bk7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The ribonuclease MC1 (RNase MC1) from seeds of bitter gourd (Momordica charantia) consists of 190 amino acid residues with four disulfide bridges and belongs to the RNase T(2) family, including fungal RNases typified by RNase Rh from Rhizopus niveus and RNase T(2) from Aspergillus oryzae. The crystal structure of RNase MC1 has been determined at 1.75 A resolution with an R-factor of 19.7% using the single isomorphous replacement method. RNase MC1 structurally belongs to the (alpha+beta) class of proteins, having ten helices (six alpha-helices and four 3(10)-helices) and eight beta-strands. When the structures of RNase MC1 and RNase Rh are superposed, the close agreement between the alpha-carbon positions for the total structure is obvious: the root mean square deviations calculated only for structurally related 151 alpha-carbon atoms of RNase MC1 and RNase Rh molecules was 1.76 A. Furthermore, the conformation of the catalytic residues His-46, Glu-105, and His-109 in RNase Rh can be easily superposed with that of the possible catalytic residues His-34, Glu-84, and His-88 in RNase MC1. This observation strongly indicates that RNase MC1 from a plant origin catalyzes RNA degradation in a similar manner as fungal RNases.
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==About this Structure==
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Crystal structure of a ribonuclease from the seeds of bitter gourd (Momordica charantia) at 1.75 A resolution.,Nakagawa A, Tanaka I, Sakai R, Nakashima T, Funatsu G, Kimura M Biochim Biophys Acta. 1999 Aug 17;1433(1-2):253-60. PMID:10446375<ref>PMID:10446375</ref>
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1BK7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Momordica_charantia Momordica charantia]. Active as [http://en.wikipedia.org/wiki/Ribonuclease_T(2) Ribonuclease T(2)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.1 3.1.27.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BK7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of a ribonuclease from the seeds of bitter gourd (Momordica charantia) at 1.75 A resolution., Nakagawa A, Tanaka I, Sakai R, Nakashima T, Funatsu G, Kimura M, Biochim Biophys Acta. 1999 Aug 17;1433(1-2):253-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10446375 10446375]
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</div>
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[[Category: Momordica charantia]]
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<div class="pdbe-citations 1bk7" style="background-color:#fffaf0;"></div>
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[[Category: Ribonuclease T(2)]]
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[[Category: Single protein]]
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[[Category: Nakagawa, A.]]
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[[Category: Tanaka, I.]]
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[[Category: hydrolase (nucleic acid]]
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[[Category: rna)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:43:08 2007''
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==See Also==
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*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Momordica charantia]]
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[[Category: Nakagawa A]]
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[[Category: Tanaka I]]

Current revision

RIBONUCLEASE MC1 FROM THE SEEDS OF BITTER GOURD

PDB ID 1bk7

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