1amm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:31, 7 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1amm.jpg|left|200px]]
 
-
{{Structure
+
==1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K==
-
|PDB= 1amm |SIZE=350|CAPTION= <scene name='initialview01'>1amm</scene>, resolution 1.2&Aring;
+
<StructureSection load='1amm' size='340' side='right'caption='[[1amm]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
-
|SITE=
+
== Structural highlights ==
-
|LIGAND=
+
<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>
-
|ACTIVITY=
+
</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>
-
|GENE=
+
<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>
-
}}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/CRGB_BOVIN CRGB_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/am/1amm_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=1amm ConSurf].
 +
<div style="clear:both"></div>
-
'''1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K'''
+
==See Also==
-
 
+
*[[Crystallin 3D structures|Crystallin 3D structures]]
-
 
+
__TOC__
-
==Overview==
+
</StructureSection>
-
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.
+
-
 
+
-
==About this Structure==
+
-
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].
+
-
 
+
-
==Reference==
+
-
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]
+
[[Category: Bos taurus]]
[[Category: Bos taurus]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Glover, I D.]]
+
[[Category: Glover ID]]
-
[[Category: Kumaraswamy, V S.]]
+
[[Category: Kumaraswamy VS]]
-
[[Category: Lindley, P F.]]
+
[[Category: Lindley PF]]
-
[[Category: Slingsby, C.]]
+
[[Category: Slingsby C]]
-
[[Category: crystallin]]
+
-
[[Category: eye lens protein]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:35 2008''
+

Current revision

1.2 ANGSTROM STRUCTURE OF GAMMA-B CRYSTALLIN AT 150K

PDB ID 1amm

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools