1aqp

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:16, 23 October 2024) (edit) (undo)
 
(16 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1aqp.jpg|left|200px]]
 
-
{{Structure
+
==RIBONUCLEASE A COPPER COMPLEX==
-
|PDB= 1aqp |SIZE=350|CAPTION= <scene name='initialview01'>1aqp</scene>, resolution 2.0&Aring;
+
<StructureSection load='1aqp' size='340' side='right'caption='[[1aqp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=CII:Cu+Binding+Site+II'>CII</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>
+
<table><tr><td colspan='2'>[[1aqp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AQP FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </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]] 2&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</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=1aqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqp OCA], [https://pdbe.org/1aqp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aqp RCSB], [https://www.ebi.ac.uk/pdbsum/1aqp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aqp ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aqp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aqp OCA], [http://www.ebi.ac.uk/pdbsum/1aqp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aqp RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/RNAS1_BOVIN RNAS1_BOVIN] Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single stranded and double stranded RNA.<ref>PMID:7479688</ref>
 +
== 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/aq/1aqp_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=1aqp ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
We report the crystal structures of the copper and nickel complexes of RNase A. The overall topology of these two complexes is similar to that of other RNase A structures. However, there are significant differences in the mode of binding of copper and nickel. There are two copper ions per molecule of the protein, but there is only one nickel ion per molecule of the protein. Significant changes occur in the interprotein interactions as a result of differences in the coordinating groups at the common binding site around His-105. Consequently, the copper- and nickel-ion-bound dimers of RNase A act as nucleation sites for generating different crystal lattices for the two complexes. A second copper ion is present at an active site residue His-119 for which all the ligands are from one molecule of the protein. At this second site, His-119 adopts an inactive conformation (B) induced by the copper. We have identified a novel copper binding motif involving the alpha-amino group and the N-terminal residues.
-
'''RIBONUCLEASE A COPPER COMPLEX'''
+
Crystal structures of the copper and nickel complexes of RNase A: metal-induced interprotein interactions and identification of a novel copper binding motif.,Balakrishnan R, Ramasubbu N, Varughese KI, Parthasarathy R Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9620-5. PMID:9275172<ref>PMID:9275172</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1aqp" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
We report the crystal structures of the copper and nickel complexes of RNase A. The overall topology of these two complexes is similar to that of other RNase A structures. However, there are significant differences in the mode of binding of copper and nickel. There are two copper ions per molecule of the protein, but there is only one nickel ion per molecule of the protein. Significant changes occur in the interprotein interactions as a result of differences in the coordinating groups at the common binding site around His-105. Consequently, the copper- and nickel-ion-bound dimers of RNase A act as nucleation sites for generating different crystal lattices for the two complexes. A second copper ion is present at an active site residue His-119 for which all the ligands are from one molecule of the protein. At this second site, His-119 adopts an inactive conformation (B) induced by the copper. We have identified a novel copper binding motif involving the alpha-amino group and the N-terminal residues.
+
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1AQP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AQP OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Crystal structures of the copper and nickel complexes of RNase A: metal-induced interprotein interactions and identification of a novel copper binding motif., Balakrishnan R, Ramasubbu N, Varughese KI, Parthasarathy R, Proc Natl Acad Sci U S A. 1997 Sep 2;94(18):9620-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9275172 9275172]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Pancreatic ribonuclease]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Ramasubbu N]]
-
[[Category: Ramasubbu, N.]]
+
-
[[Category: hydrolase (phosphoric diester)]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:45:43 2008''
+

Current revision

RIBONUCLEASE A COPPER COMPLEX

PDB ID 1aqp

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools