1hy0: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /><applet load="1hy0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hy0, resolution 2.20Å" /> '''CRYSTAL STRUCTURE OF...
 
No edit summary
 
(14 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1hy0.jpg|left|200px]]<br /><applet load="1hy0" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hy0, resolution 2.20&Aring;" />
'''CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 1 CRYSTALLIN (EYE LENS PROTEIN)'''<br />


==Overview==
==CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 1 CRYSTALLIN (EYE LENS PROTEIN)==
Duck delta1 and delta2 crystallin are 94% identical in amino acid, sequence, and while delta2 crystallin is the duck orthologue of, argininosuccinate lyase (ASL) and catalyzes the reversible breakdown of, argininosuccinate to arginine and fumarate, the delta1 isoform is, enzymatically inactive. The crystal structures of wild type duck delta1, and delta2 crystallin have been solved at 2.2 and 2.3 A resolution, respectively, and the refinement of the turkey delta1 crystallin has been, completed. These structures have been compared with two mutant duck delta2, crystallin structures. Conformational changes were observed in two regions, of the N-terminal domain with intraspecies differences between the active, and inactive isoforms localized to residues 23-32 and both intra- and, interspecies differences localized to the loop of residues 74-89. As the, residues implicated in the catalytic mechanism of delta2/ASL are all, conserved in delta1, the amino acid substitutions in these two regions are, hypothesized to be critical for substrate binding. A sulfate anion was, found in the active site of duck delta1 crystallin. This anion, which, appears to mimic the fumarate moiety of the argininosuccinate substrate, induces a rigid body movement in domain 3 and a conformational change in, the loop of residues 280-290, which together would sequester the substrate, from the solvent. The duck delta1 crystallin structure suggests that Ser, 281, a residue strictly conserved in all members of the superfamily, could, be the catalytic acid in the delta2 crystallin/ASL enzymatic mechanism.
<StructureSection load='1hy0' size='340' side='right'caption='[[1hy0]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hy0]] is a 2 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=1HY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HY0 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1hy0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy0 OCA], [https://pdbe.org/1hy0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hy0 RCSB], [https://www.ebi.ac.uk/pdbsum/1hy0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hy0 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ARLY1_ANAPL ARLY1_ANAPL] Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. Despite possessing the necessary catalytic residues, this protein does not function as an enzymatically active argininosuccinate lyase.<ref>PMID:7944404</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/hy/1hy0_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=1hy0 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1HY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anas_platyrhynchos Anas platyrhynchos] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HY0 OCA].
*[[Crystallin 3D structures|Crystallin 3D structures]]
 
== References ==
==Reference==
<references/>
Structural studies of duck delta 1 and delta 2 crystallin suggest conformational changes occur during catalysis., Sampaleanu LM, Vallee F, Slingsby C, Howell PL, Biochemistry. 2001 Mar 6;40(9):2732-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11258884 11258884]
__TOC__
</StructureSection>
[[Category: Anas platyrhynchos]]
[[Category: Anas platyrhynchos]]
[[Category: Argininosuccinate lyase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Howell PL]]
[[Category: Howell, P.L.]]
[[Category: Sampaleanu LM]]
[[Category: Sampaleanu, L.M.]]
[[Category: Slingsby C]]
[[Category: Slingsby, C.]]
[[Category: Vallee F]]
[[Category: Vallee, F.]]
[[Category: SO4]]
[[Category: argininosuccinate lyase]]
[[Category: delta 1 crystallin]]
[[Category: eye lens protein]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:54:05 2007''

Latest revision as of 10:31, 7 February 2024

CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 1 CRYSTALLIN (EYE LENS PROTEIN)CRYSTAL STRUCTURE OF WILD TYPE DUCK DELTA 1 CRYSTALLIN (EYE LENS PROTEIN)

Structural highlights

1hy0 is a 2 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 2.2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARLY1_ANAPL Delta crystallin, the principal crystallin in embryonic lens, is found only in birds and reptiles. Despite possessing the necessary catalytic residues, this protein does not function as an enzymatically active argininosuccinate lyase.[1]

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. ↑ Lee HJ, Lin CC, Chiou SH, Chang GG. Characterization of the multiple forms of duck lens delta-crystallin with endogenous argininosuccinate lyase activity. Arch Biochem Biophys. 1994 Oct;314(1):31-8. PMID:7944404 doi:http://dx.doi.org/10.1006/abbi.1994.1408

1hy0, resolution 2.20Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1hy0&oldid=4044688"