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<StructureSection load='1mgw' size='340' side='right'caption='[[1mgw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1mgw' size='340' side='right'caption='[[1mgw]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1mgw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_10762 Atcc 10762]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGW FirstGlance]. <br>
<table><tr><td colspan='2'>[[1mgw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Kitasatospora_aureofaciens Kitasatospora aureofaciens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGW FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI:LITHIUM+ION'>LI</scene></td></tr>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rgg|1rgg]], [[1mgr|1mgr]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LI:LITHIUM+ION'>LI</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Ribonuclease_T(1) Ribonuclease T(1)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.3 3.1.27.3] </span></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=1mgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgw OCA], [https://pdbe.org/1mgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgw RCSB], [https://www.ebi.ac.uk/pdbsum/1mgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgw ProSAT]</span></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=1mgw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgw OCA], [https://pdbe.org/1mgw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgw RCSB], [https://www.ebi.ac.uk/pdbsum/1mgw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgw ProSAT]</span></td></tr>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNS3_KITAU RNS3_KITAU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1mgw ConSurf].
</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=1mgw ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ribonuclease (RNase) Sa3 is secreted by the Gram-positive bacterium Streptomyces aureofaciens. The enzyme catalyzes the cleavage of RNA on the 3' side of guanosine residues. Here, x-ray diffraction analysis was used to determine the three-dimensional structure of two distinct crystalline forms of RNase Sa3 to a resolution of 2.0 and 1.7 A. These two structures are similar to each other as well as to that of a homolog, RNase Sa. All of the key active-site residues of RNase Sa (Asn(42), Glu(44), Glu(57), Arg(72), and His(88)) are located in the putative active site of RNase Sa3. Also herein, RNase Sa3 is shown to be toxic to human erythroleukemia cells in culture. Like onconase, which is an amphibian ribonuclease in Phase III clinical trials as a cancer chemotherapeutic, RNase Sa3 is not inhibited by the cytosolic ribonuclease inhibitor protein. Thus, a prokaryotic ribonuclease can be toxic to mammalian cells.
X-ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity.,Sevcik J, Urbanikova L, Leland PA, Raines RT J Biol Chem. 2002 Dec 6;277(49):47325-30. Epub 2002 Sep 11. PMID:12228255<ref>PMID:12228255</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1mgw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 10762]]
[[Category: Kitasatospora aureofaciens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Leland, P A]]
[[Category: Leland PA]]
[[Category: Raines, R T]]
[[Category: Raines RT]]
[[Category: Sevcik, J]]
[[Category: Sevcik J]]
[[Category: Urbanikova, L]]
[[Category: Urbanikova L]]
[[Category: Alpha/beta protein]]
[[Category: Hydrolase]]
[[Category: Ub roll]]

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