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[[Image:1n1x.gif|left|200px]]<br /><applet load="1n1x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1n1x, resolution 1.45&Aring;" />
'''Crystal Structure Analysis of the monomeric [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32] Bovine seminal ribonuclease'''<br />


==Overview==
==Crystal Structure Analysis of the monomeric [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32] Bovine seminal ribonuclease==
Bovine seminal ribonuclease, a homodimeric enzyme joined covalently by two interchain disulphide bonds, is an equilibrium mixture of two conformational isomers, MxM and M=M. The major form, MxM, whose crystal structure has been previously determined at 1.9 A resolution, presents the swapping of the N-terminal segments (residues 1-15) and composite active sites formed by residues of different chains. The three-dimensional domain swapping does not occur in the M=M form. The different fold of each N-terminal tail is directed by the hinge loop (residue 16-22) connecting the swapping domain to the body of the protein. Reduction and alkylation of interchain disulphide bridges produce a monomeric derivative and a noncovalent swapped dimer, which are both active. The free and nucleotide-bound forms of the monomer have been crystallized at an alkaline pH and refined at 1.45 and 1.65 A resolution, respectively. In both cases, the N-terminal fragment is folded on the main body of the protein to produce an intact active site and a chain architecture very similar to that of bovine pancreatic ribonuclease. In this new fold of the seminal chain, the hinge loop is disordered. Despite the difference between the tertiary structure of the monomer and that of the chains in the MxM form, the active sites of the two enzymes are virtually indistinguishable. Furthermore, the structure of the liganded enzyme represents the first example of a ribonuclease complex studied at an alkaline pH and provides new information on the binding of a nucleotide when the catalytic histidines are deprotonated.
<StructureSection load='1n1x' size='340' side='right'caption='[[1n1x]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1n1x]] 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=1N1X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N1X FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=YCM:S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE'>YCM</scene></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=1n1x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n1x OCA], [https://pdbe.org/1n1x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n1x RCSB], [https://www.ebi.ac.uk/pdbsum/1n1x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n1x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/RNS_BOVIN RNS_BOVIN] This enzyme hydrolyzes both single- and double-stranded RNA.
== 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/n1/1n1x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1n1x ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1N1X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N1X OCA].
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The unswapped chain of bovine seminal ribonuclease: Crystal structure of the free and liganded monomeric derivative., Sica F, Di Fiore A, Zagari A, Mazzarella L, Proteins. 2003 Aug 1;52(2):263-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12833549 12833549]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Pancreatic ribonuclease]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Di Fiore A]]
[[Category: Fiore, A Di.]]
[[Category: Mazzarella L]]
[[Category: Mazzarella, L.]]
[[Category: Sica F]]
[[Category: Sica, F.]]
[[Category: Zagari A]]
[[Category: Zagari, A.]]
[[Category: hydrolase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:19 2008''

Latest revision as of 11:44, 10 April 2024

Crystal Structure Analysis of the monomeric [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32] Bovine seminal ribonucleaseCrystal Structure Analysis of the monomeric [S-carboxyamidomethyl-Cys31, S-carboxyamidomethyl-Cys32] Bovine seminal ribonuclease

Structural highlights

1n1x is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.45Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RNS_BOVIN This enzyme hydrolyzes both single- and double-stranded RNA.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1n1x, resolution 1.45Å

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