1hy1

<table><tr><td colspan='2'>[[1hy1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Anapl Anapl]. The July 2010 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Crystallins'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2010_7 10.2210/rcsb_pdb/mom_2010_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HY1 FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1auw|1auw]], [[1dcn|1dcn]], [[1aos|1aos]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Argininosuccinate_lyase Argininosuccinate lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.2.1 4.3.2.1] </span></td></tr>

[[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>

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== Publication Abstract from PubMed ==

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.

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:11258884<ref>PMID:11258884</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1hy1" style="background-color:#fffaf0;"></div>

[[Category: Anapl]]

[[Category: Argininosuccinate lyase]]

[[Category: Howell, P L]]

[[Category: Sampaleanu, L M]]

[[Category: Slingsby, C]]

[[Category: Vallee, F]]

[[Category: Lyase]]