1iqq: Difference between revisions

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-[[Image:1iqq.jpg|left|200px]]
- {{Structure
+==Crystal Structure of Japanese pear S3-RNase==
-|PDB= 1iqq |SIZE=350|CAPTION= <scene name='initialview01'>1iqq</scene>, resolution 1.50&Aring;
+<StructureSection load='1iqq' size='340' side='right'caption='[[1iqq]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene>
+<table><tr><td colspan='2'>[[1iqq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrus_pyrifolia Pyrus pyrifolia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IQQ FirstGlance]. <br>
-|ACTIVITY= <span class='plainlinks'>[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] </span>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1iqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqq OCA], [https://pdbe.org/1iqq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iqq RCSB], [https://www.ebi.ac.uk/pdbsum/1iqq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iqq ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1iqq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iqq OCA], [http://www.ebi.ac.uk/pdbsum/1iqq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1iqq RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/RNS3_PYRPY RNS3_PYRPY] Self-incompatibility (SI) is the inherited ability of a flowering plant to prevent self-fertilization by discriminating between self and non-self pollen during pollination. In many species, self-incompatibility is controlled by the single, multiallelic locus S.
+== 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/iq/1iqq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1iqq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The crystal structure of the Pyrus pyrifolia pistil ribonuclease (S(3)-RNase) responsible for gametophytic self-incompatibility was determined at 1.5-A resolution. It consists of eight helices and seven beta-strands, and its folding topology is typical of RNase T(2) family enzymes. Based on a structural comparison of S(3)-RNase with RNase Rh, a fungal RNase T(2) family enzyme, the active site residues of S(3)-RNase assigned were His(33) and His(88) as catalysts and Glu(84) and Lys(87) as stabilizers of an intermediate in the transition state. Moreover, amino acid residues that constitute substrate binding sites of the two RNases could be superimposed geometrically. A hypervariable (HV) region that has an S-allele-specific sequence comprises a long loop and short alpha-helix. This region is far from the active site cleft, exposed on the molecule's surface, and positively charged. Four positively selected (PS) regions, in which the number of nonsynonymous substitutions exceeds that of synonymous ones, are located on either side of the active site cleft, and accessible to solvent. These structural features suggest that the HV or PS regions may interact with a pollen S-gene product(s) to recognize self and non-self pollen.
-'''Crystal Structure of Japanese pear S3-RNase'''
+Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility.,Matsuura T, Sakai H, Unno M, Ida K, Sato M, Sakiyama F, Norioka S J Biol Chem. 2001 Nov 30;276(48):45261-9. Epub 2001 Sep 27. PMID:11577107<ref>PMID:11577107</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1iqq" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-The crystal structure of the Pyrus pyrifolia pistil ribonuclease (S(3)-RNase) responsible for gametophytic self-incompatibility was determined at 1.5-A resolution. It consists of eight helices and seven beta-strands, and its folding topology is typical of RNase T(2) family enzymes. Based on a structural comparison of S(3)-RNase with RNase Rh, a fungal RNase T(2) family enzyme, the active site residues of S(3)-RNase assigned were His(33) and His(88) as catalysts and Glu(84) and Lys(87) as stabilizers of an intermediate in the transition state. Moreover, amino acid residues that constitute substrate binding sites of the two RNases could be superimposed geometrically. A hypervariable (HV) region that has an S-allele-specific sequence comprises a long loop and short alpha-helix. This region is far from the active site cleft, exposed on the molecule's surface, and positively charged. Four positively selected (PS) regions, in which the number of nonsynonymous substitutions exceeds that of synonymous ones, are located on either side of the active site cleft, and accessible to solvent. These structural features suggest that the HV or PS regions may interact with a pollen S-gene product(s) to recognize self and non-self pollen.
+*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-IQQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Pyrus_pyrifolia Pyrus pyrifolia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IQQ OCA].
+__TOC__
+</StructureSection>
-==Reference==
+[[Category: Large Structures]]
-Crystal structure at 1.5-A resolution of Pyrus pyrifolia pistil ribonuclease responsible for gametophytic self-incompatibility., Matsuura T, Sakai H, Unno M, Ida K, Sato M, Sakiyama F, Norioka S, J Biol Chem. 2001 Nov 30;276(48):45261-9. Epub 2001 Sep 27. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11577107 11577107]
 [[Category: Pyrus pyrifolia]]
-[[Category: Ribonuclease T(2)]]
+[[Category: Matsuura T]]
-[[Category: Single protein]]
+[[Category: Norioka S]]
-[[Category: Matsuura, T.]]
+[[Category: Sakai H]]
-[[Category: Norioka, S.]]
-[[Category: Sakai, H.]]
-[[Category: hydrolase]]
-[[Category: japanese pear]]
-[[Category: pyrus pyrifolia]]
-[[Category: s-rnase]]
-[[Category: self-incompatibility]]
-[[Category: t2 family ribonuclease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:20 2008''