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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]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:51:39 2007''

Latest revision as of 09:33, 7 February 2024

H91N DELTA 2 CRYSTALLIN FROM DUCKH91N DELTA 2 CRYSTALLIN FROM DUCK

Structural highlights

1auw is a 4 chain structure with sequence from Anas platyrhynchos. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.[1] [2] [3] [4]

Evolutionary Conservation

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

See Also

References

  1. ↑ Vallee F, Turner MA, Lindley PL, Howell PL. Crystal structure of an inactive duck delta II crystallin mutant with bound argininosuccinate. Biochemistry. 1999 Feb 23;38(8):2425-34. PMID:10029536 doi:10.1021/bi982149h
  2. ↑ Sampaleanu LM, Yu B, Howell PL. Mutational analysis of duck delta 2 crystallin and the structure of an inactive mutant with bound substrate provide insight into the enzymatic mechanism of argininosuccinate lyase. J Biol Chem. 2002 Feb 8;277(6):4166-75. Epub 2001 Nov 6. PMID:11698398 doi:10.1074/jbc.M107465200
  3. ↑ Sampaleanu LM, Codding PW, Lobsanov YD, Tsai M, Smith GD, Horvatin C, Howell PL. Structural studies of duck delta2 crystallin mutants provide insight into the role of Thr161 and the 280s loop in catalysis. Biochem J. 2004 Dec 1;384(Pt 2):437-47. PMID:15320872 doi:10.1042/BJ20040656
  4. ↑ Abu-Abed M, Turner MA, Vallee F, Simpson A, Slingsby C, Howell PL. Structural comparison of the enzymatically active and inactive forms of delta crystallin and the role of histidine 91. Biochemistry. 1997 Nov 18;36(46):14012-22. PMID:9369472 doi:10.1021/bi971407s

1auw, resolution 2.50Å

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