1blb: Difference between revisions

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New page: left|200px<br /><applet load="1blb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1blb, resolution 3.3Å" /> '''CLOSE PACKING OF AN O...
 
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[[Image:1blb.gif|left|200px]]<br /><applet load="1blb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1blb, resolution 3.3&Aring;" />
'''CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS'''<br />


==Overview==
==CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS==
beta-Crystallins are oligomeric eye lens proteins that are related to, monomeric gamma-crystallins. The main sequence difference between the two, families is the presence of sequence extensions in the beta-crystallins. A, major question concerns the role that these extensions play in mediating, interactions at the high protein concentrations found in the lens. The, predominant beta-crystallin polypeptide, beta B2, can be crystallized in, two different space groups, I222 and C222. The I222 crystal structure, revealed that the protein packed as a tetramer with perfect 222 symmetry, but that the extensions were disordered. The X-ray structure of the C222, lattice of beta B2 has now been refined at 3.3 A, the structure analysed, and compared with the I222 lattice. The protein is also a tetramer with, 222 symmetry in the C222 lattice but differs in that parts of the, N-terminal extensions have been visualized. In the asymmetric unit of the, C222 lattice there are four subunits, each comprising a single polypeptide, chain, in which certain flexible loops in the N-terminal domains and the, N-terminal extensions have various conformations. The tetramers in the, C222 lattice are more tightly packed than in the I222 form. Analysis of, the tetramer contacts shows that the sites of interaction break the 222, symmetry of the tetramers. The N-terminal extensions play a major role in, directing interactions between tetramers. One of the N-terminal extensions, interacts with a hydrophobic patch on the N-terminal domain of another, tetramer. These crystallographic observations obtained over a, physiological concentration range indicate how, in beta-crystallin, oligomers, the N-terminal extensions of beta B2 can switch from, interacting with water to interacting with protein depending on their, relative concentrations. This could be useful in maintaining a gradient of, refractive index.
<StructureSection load='1blb' size='340' side='right'caption='[[1blb]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1blb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. The July 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Crystallins''  by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_7 10.2210/rcsb_pdb/mom_2010_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BLB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BLB 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]] 3.3&#8491;</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=1blb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1blb OCA], [https://pdbe.org/1blb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1blb RCSB], [https://www.ebi.ac.uk/pdbsum/1blb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1blb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CRBB2_BOVIN CRBB2_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens.
== 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/bl/1blb_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=1blb ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BLB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BLB OCA].
*[[Crystallin 3D structures|Crystallin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Close packing of an oligomeric eye lens beta-crystallin induces loss of symmetry and ordering of sequence extensions., Nalini V, Bax B, Driessen H, Moss DS, Lindley PF, Slingsby C, J Mol Biol. 1994 Mar 4;236(4):1250-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8120900 8120900]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Crystallins]]
[[Category: Bax, B.]]
[[Category: Large Structures]]
[[Category: Driessen, H.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Lindley, P.F.]]
[[Category: Bax B]]
[[Category: Moss, D.S.]]
[[Category: Driessen H]]
[[Category: Nalini, V.]]
[[Category: Lindley PF]]
[[Category: Slingsby, C.]]
[[Category: Moss DS]]
[[Category: eye lens protein]]
[[Category: Nalini V]]
 
[[Category: Slingsby C]]
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:44:21 2007''

Latest revision as of 09:37, 7 February 2024

CLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONSCLOSE PACKING OF AN OLIGOMERIC EYE LENS BETA-CRYSTALLIN INDUCES LOSS OF SYMMETRY AND ORDERING OF SEQUENCE EXTENSIONS

Structural highlights

1blb is a 4 chain structure with sequence from Bos taurus. The July 2010 RCSB PDB Molecule of the Month feature on Crystallins by David Goodsell is 10.2210/rcsb_pdb/mom_2010_7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CRBB2_BOVIN Crystallins are the dominant structural components of the vertebrate eye lens.

Evolutionary Conservation

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

See Also

1blb, resolution 3.30Å

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