View source for 7ljh


==Structure of poly(aspartic acid) hydrolase PahZ2 with Zn+2 bound==
<StructureSection load='7ljh' size='340' side='right'caption='[[7ljh]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ljh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sphingomonas_sp._KT-1 Sphingomonas sp. KT-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LJH 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7ljh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ljh OCA], [https://pdbe.org/7ljh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ljh RCSB], [https://www.ebi.ac.uk/pdbsum/7ljh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ljh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q769D3_9SPHN Q769D3_9SPHN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Poly(aspartic acid) (PAA) is a common water-soluble polycarboxylate used in a broad range of applications. PAA biodegradation and environmental assimilation were first identified in river water bacterial strains, Sphingomonas sp. KT-1 and Pedobacter sp. KP-2. Within Sphingomonas sp. KT-1, PahZ1KT-1 cleaves beta-amide linkages to oligo(aspartic acid) and then is degraded by PahZ2KT-1. Recently, we reported the first structure for PahZ1KT-1. Here, we report novel structures for PahZ2KT-1 bound to either Gd(3+)/Sm(3+) or Zn(2+) cations in a dimeric state consistent with M28 metallopeptidase family members. PahZ2KT-1 monomers include a dimerization domain and a catalytic domain with dual Zn(2+) cations. MD methods predict the putative substrate binding site to span across the dimerization and catalytic domains, where NaCl promotes the transition from an open conformation to a closed conformation that positions the substrate adjacent to catalytic zinc ions. Structural knowledge of PahZ1KT-1 and PahZ2KT-1 will allow for protein engineering endeavors to develop novel biodegradation reagents.

Sphingomonas sp. KT-1 PahZ2 Structure Reveals a Role for Conformational Dynamics in Peptide Bond Hydrolysis.,Brambley CA, Yared TJ, Gonzalez M, Jansch AL, Wallen JR, Weiland MH, Miller JM J Phys Chem B. 2021 Jun 10;125(22):5722-5739. doi: 10.1021/acs.jpcb.1c01216. Epub, 2021 Jun 1. PMID:34060838<ref>PMID:34060838</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ljh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sphingomonas sp. KT-1]]
[[Category: Brambley CA]]
[[Category: Gonzalez M]]
[[Category: Jansch AL]]
[[Category: Miller JM]]
[[Category: Wallen JR]]
[[Category: Weiland MH]]
[[Category: Yared TJ]]