1y44

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:56, 6 November 2024) (edit) (undo)
 
(14 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1y44.gif|left|200px]]
 
-
{{Structure
+
==Crystal structure of RNase Z==
-
|PDB= 1y44 |SIZE=350|CAPTION= <scene name='initialview01'>1y44</scene>, resolution 2.10&Aring;
+
<StructureSection load='1y44' size='340' side='right'caption='[[1y44]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
+
<table><tr><td colspan='2'>[[1y44]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y44 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y44 FirstGlance]. <br>
-
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_Z Ribonuclease Z], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.11 3.1.26.11] </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]] 2.1&#8491;</td></tr>
-
|GENE= rnz ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1y44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y44 OCA], [https://pdbe.org/1y44 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y44 RCSB], [https://www.ebi.ac.uk/pdbsum/1y44 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y44 ProSAT]</span></td></tr>
-
|RELATEDENTRY=
+
</table>
-
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1y44 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y44 OCA], [http://www.ebi.ac.uk/pdbsum/1y44 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1y44 RCSB]</span>
+
== Function ==
-
}}
+
[https://www.uniprot.org/uniprot/RNZ_BACSU RNZ_BACSU] Zinc phosphodiesterase, which displays some tRNA 3'-processing endonuclease activity. Probably involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA.<ref>PMID:12941704</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/y4/1y44_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=1y44 ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
Transfer RNAs (tRNAs) are synthesized as part of longer primary transcripts that require processing of both their 3' and 5' extremities in every living organism known. The 5' side is processed (matured) by the ubiquitously conserved endonucleolytic ribozyme, RNase P, whereas removal of the 3' tails can be either exonucleolytic or endonucleolytic. The endonucleolytic pathway is catalysed by an enzyme known as RNase Z, or 3' tRNase. RNase Z cleaves precursor tRNAs immediately after the discriminator base (the unpaired nucleotide 3' to the last base pair of the acceptor stem, used as an identity determinant by many aminoacyl-tRNA synthetases) in most cases, yielding a tRNA primed for addition of the CCA motif by nucleotidyl transferase. Here we report the crystal structure of Bacillus subtilis RNase Z at 2.1 A resolution, and propose a mechanism for tRNA recognition and cleavage. The structure explains the allosteric properties of the enzyme, and also sheds light on the mechanisms of inhibition by the CCA motif and long 5' extensions. Finally, it highlights the extraordinary adaptability of the metallo-hydrolase domain of the beta-lactamase family for the hydrolysis of covalent bonds.
-
'''Crystal structure of RNase Z'''
+
Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z.,de la Sierra-Gallay IL, Pellegrini O, Condon C Nature. 2005 Feb 10;433(7026):657-61. Epub 2005 Jan 16. PMID:15654328<ref>PMID:15654328</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1y44" style="background-color:#fffaf0;"></div>
-
==Overview==
+
==See Also==
-
Transfer RNAs (tRNAs) are synthesized as part of longer primary transcripts that require processing of both their 3' and 5' extremities in every living organism known. The 5' side is processed (matured) by the ubiquitously conserved endonucleolytic ribozyme, RNase P, whereas removal of the 3' tails can be either exonucleolytic or endonucleolytic. The endonucleolytic pathway is catalysed by an enzyme known as RNase Z, or 3' tRNase. RNase Z cleaves precursor tRNAs immediately after the discriminator base (the unpaired nucleotide 3' to the last base pair of the acceptor stem, used as an identity determinant by many aminoacyl-tRNA synthetases) in most cases, yielding a tRNA primed for addition of the CCA motif by nucleotidyl transferase. Here we report the crystal structure of Bacillus subtilis RNase Z at 2.1 A resolution, and propose a mechanism for tRNA recognition and cleavage. The structure explains the allosteric properties of the enzyme, and also sheds light on the mechanisms of inhibition by the CCA motif and long 5' extensions. Finally, it highlights the extraordinary adaptability of the metallo-hydrolase domain of the beta-lactamase family for the hydrolysis of covalent bonds.
+
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
-
 
+
== References ==
-
==About this Structure==
+
<references/>
-
1Y44 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y44 OCA].
+
__TOC__
-
 
+
</StructureSection>
-
==Reference==
+
-
Structural basis for substrate binding, cleavage and allostery in the tRNA maturase RNase Z., de la Sierra-Gallay IL, Pellegrini O, Condon C, Nature. 2005 Feb 10;433(7026):657-61. Epub 2005 Jan 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15654328 15654328]
+
[[Category: Bacillus subtilis]]
[[Category: Bacillus subtilis]]
-
[[Category: Ribonuclease Z]]
+
[[Category: Large Structures]]
-
[[Category: Single protein]]
+
[[Category: Condon C]]
-
[[Category: Condon, C.]]
+
[[Category: Pellegrini O]]
-
[[Category: Pellegrini, O.]]
+
[[Category: De la Sierra-Gallay IL]]
-
[[Category: Sierra-Gallay, I L.de la.]]
+
-
[[Category: zinc-dependent metal hydrolase]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:58:31 2008''
+

Current revision

Crystal structure of RNase Z

PDB ID 1y44

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools