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==H91N DELTA 2 CRYSTALLIN FROM DUCK==
==H91N DELTA 2 CRYSTALLIN FROM DUCK==
<StructureSection load='1auw' size='340' side='right' caption='[[1auw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1auw' size='340' side='right'caption='[[1auw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1auw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Anapl Anapl]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AUW FirstGlance]. <br>
<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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1auw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1auw OCA], [http://pdbe.org/1auw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1auw RCSB], [http://www.ebi.ac.uk/pdbsum/1auw PDBsum]</span></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>
</table>
== Function ==
== Function ==
[[http://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>
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/au/1auw_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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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=1auw ConSurf].
</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>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 reexamination of the kinetic properties of the H91N mutant reveals that the mutant has 10% wild-type activity. The Vmax of the mutant protein is identical to that of the wild-type protein, but a 10-fold increase in the Michaelis constant is seen, suggesting that His 91 is involved in binding the substrate. In an effort to determine the reasons for the loss of enzymatic activity in delta I crystallin, a structural comparison of the H91N mutant with the enzymatically inactive turkey delta I crystallin has been performed. This study revealed a remarkable similarity in the overall structures of the two proteins. Three regions of secondary structure do differ significantly between the two models; these include the N-terminal tail, a loop containing residues 76-91, and a cis versus trans peptide linkage at residue Thr 322. The cis to trans peptide variation appears to be an interspecies difference between turkey and duck and is therefore not directly involved in the loss of enzymatic activity. All the residues implicated in the catalytic mechanism are conserved in both the active and inactive proteins, and given the linearity of the relationship between the enzymatic activity of duck delta I/delta II heterotetramers and their delta II content (Piatigorsky &amp; Horwitz, 1996), it is evident from the structure that only one of the three domains that contributes to the active site is responsible for the loss of activity in the delta I protein. Given the structural differences found in domain 1 (N-terminal tail and 76-91 loop), we postulate that these differences are responsible for the loss of catalytic activity in the delta I crystallin protein and that the delta I protein is inactive because it no longer binds the substrate.
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:9369472<ref>PMID:9369472</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1auw" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Crystalline|Crystalline]]
*[[Crystallin 3D structures|Crystallin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Anapl]]
[[Category: Anas platyrhynchos]]
[[Category: Argininosuccinate lyase]]
[[Category: Large Structures]]
[[Category: Abu-Abed, M]]
[[Category: Abu-Abed M]]
[[Category: Howell, P L]]
[[Category: Howell PL]]
[[Category: Vallee, F]]
[[Category: Vallee F]]
[[Category: Arginosuccinate lyase]]
[[Category: Delta 2 crystallin]]
[[Category: Eye lens protein]]

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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