1auw: Difference between revisions

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[[Image:1auw.gif|left|200px]]<br />
<applet load="1auw" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1auw, resolution 2.5&Aring;" />
'''H91N DELTA 2 CRYSTALLIN FROM DUCK'''<br />


==Overview==
==H91N DELTA 2 CRYSTALLIN FROM DUCK==
The major soluble protein component of avian and reptilian eye lenses, delta crystallin, is highly homologous to the urea cycle enzyme, argininosuccinate lyase (ASL). In duck lenses there are two highly, homologous delta crystallins, termed delta I and delta II, that are 94%, identical in amino acid sequence. While delta II crystallin has been shown, to exhibit ASL activity in vitro, delta I crystallin is inactive. The, X-ray structure of a His to Asn mutant of duck delta II crystallin (H91N), has been determined to 2.5 A resolution using the molecular replacement, technique. The overall fold of the protein is similar to other members of, the superfamily to which this protein belongs, with the active site, located in a cleft between three different monomers of the tetrameric, protein. A ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9369472 (full description)]]
<StructureSection load='1auw' size='340' side='right'caption='[[1auw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1auw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AUW 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]] 2.5&#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=1auw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auw OCA], [https://pdbe.org/1auw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1auw RCSB], [https://www.ebi.ac.uk/pdbsum/1auw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1auw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARLY2_ANAPL ARLY2_ANAPL] Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. This protein also functions as an enzymatically active argininosuccinate lyase.<ref>PMID:10029536</ref> <ref>PMID:11698398</ref> <ref>PMID:15320872</ref> <ref>PMID:9369472</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/au/1auw_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=1auw ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1AUW is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos]]. Active as [[http://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1]]. Structure known Active Sites: CAA, CAB, CAC and CAD. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AUW OCA]].
*[[Crystallin 3D structures|Crystallin 3D structures]]
 
== References ==
==Reference==
<references/>
Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91., Abu-Abed M, Turner MA, Vallee F, Simpson A, Slingsby C, Howell PL, Biochemistry. 1997 Nov 18;36(46):14012-22. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9369472 9369472]
__TOC__
</StructureSection>
[[Category: Anas platyrhynchos]]
[[Category: Anas platyrhynchos]]
[[Category: Argininosuccinate lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Abu-Abed M]]
[[Category: Abu-Abed, M.]]
[[Category: Howell PL]]
[[Category: Howell, P.L.]]
[[Category: Vallee F]]
[[Category: Vallee, F.]]
[[Category: arginosuccinate lyase]]
[[Category: delta 2 crystallin]]
[[Category: eye lens protein]]
 
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