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1amm

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[[Image:1amm.jpg|left|200px]]
 
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==1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K==
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The line below this paragraph, containing "STRUCTURE_1amm", creates the "Structure Box" on the page.
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<StructureSection load='1amm' size='340' side='right'caption='[[1amm]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1amm]] 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=1AMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AMM FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1amm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1amm OCA], [https://pdbe.org/1amm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1amm RCSB], [https://www.ebi.ac.uk/pdbsum/1amm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1amm ProSAT]</span></td></tr>
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{{STRUCTURE_1amm| PDB=1amm | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_BOVIN] Crystallins are the dominant structural components of the vertebrate eye lens.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/am/1amm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1amm ConSurf].
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<div style="clear:both"></div>
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'''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''
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==See Also==
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*[[Crystallin 3D structures|Crystallin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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gammabeta-crystallin is a structural protein of the eye lens with a role in the maintenance of an even distribution of protein and water over distances around the wavelength of light, preserving lens transparency. The structure of the 174-residue bovine protein has already been determined at room temperature to 1.47 A resolution. By flash freezing the protein crystals, data have now been collected to a nominal resolution limit of 1.2 A as radiation damage was essentially eliminated. The protein-water model has been refined against this data using the program RESTRAIN converging to an R factor of 18.5% with all data. Atomic positions are clearly indicated in the electron-density maps. Discrete bimodal disorder has been visualized for a few side chains. Out of a total of 498 water molecules present in the crystal asymmetric unit, 394 have been modelled and refined at unit occupancy. The solvent structure is extremely well ordered with an average B value of 23.4 A(2). Partially occupied sites have been identified where disorder in the protein induces concomitant disorder in the local solvent structure. The solvent structure covers 97% of the solvent-exposed surface of the protein in the crystal. 126 water molecules are distributed in second and higher hydration shells. There are networks of hydrogen-bonded solvent extending up to 64 molecules in a network, comprising trimers and tetramers as well as five- and six-membered water-ring structures. The hydration of the protein surface is dominated by arginine and aspartate side chains. Extensive cages of highly ordered solvent molecules are also observed around exposed non-polar groups.
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==About this Structure==
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1AMM 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=1AMM OCA].
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==Reference==
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An eye lens protein-water structure: 1.2 A resolution structure of gammaB-crystallin at 150 K., Kumaraswamy VS, Lindley PF, Slingsby C, Glover ID, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):611-22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299624 15299624]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Glover, I D.]]
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[[Category: Glover ID]]
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[[Category: Kumaraswamy, V S.]]
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[[Category: Kumaraswamy VS]]
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[[Category: Lindley, P F.]]
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[[Category: Lindley PF]]
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[[Category: Slingsby, C.]]
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[[Category: Slingsby C]]
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[[Category: Crystallin]]
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[[Category: Eye lens protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:27:16 2008''
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1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K

PDB ID 1amm

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