4ny5: Difference between revisions

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==X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A==
==X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A==
<StructureSection load='4ny5' size='340' side='right' caption='[[4ny5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='4ny5' size='340' side='right' caption='[[4ny5]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j1a|4j1a]], [[4j1b|4j1b]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j1a|4j1a]], [[4j1b|4j1b]]</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></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=4ny5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ny5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ny5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ny5 PDBsum]</span></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=4ny5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ny5 OCA], [http://pdbe.org/4ny5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ny5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ny5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ny5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 4ny5" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Revision as of 11:14, 5 August 2016

X-ray structure of the adduct formed between hen egg white lysozyme and NAMI-AX-ray structure of the adduct formed between hen egg white lysozyme and NAMI-A

Structural highlights

4ny5 is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Lysozyme, with EC number 3.2.1.17
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1]

Publication Abstract from PubMed

A crystallographic study of the adduct formed between hen egg white lysozyme (HEWL) and NAMI-A, an established ruthenium(iii) anticancer agent in clinical trials, is presented here. The X-ray structure reveals that NAMI-A coordinates the protein, as a naked ruthenium ion, at two distinct sites (namely Asp101 or Asp119) after releasing all its original ligands (DMSO, imidazole and Cl(-)). Structural data of the HEWL/NAMI-A adduct are compared with those previously obtained for the HEWL adduct of AziRu, a NAMI-A analogue bearing a pyridine in place of imidazole. The present results further support the view that NAMI-A exerts its biological effects acting as a classical "prodrug" first undergoing activation and then causing extensive metalation of relevant protein targets. It is also proposed that the original Ru-ligands, although absent in the final adduct, play a major role in directing the ruthenium center to its ultimate anchoring site on the protein surface.

Ruthenium metalation of proteins: the X-ray structure of the complex formed between NAMI-A and hen egg white lysozyme.,Messori L, Merlino A Dalton Trans. 2014 Mar 25;43(16):6128-31. doi: 10.1039/c3dt53582g. PMID:24553967[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Maehashi K, Matano M, Irisawa T, Uchino M, Kashiwagi Y, Watanabe T. Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white. Gene. 2012 Jan 15;492(1):244-9. doi: 10.1016/j.gene.2011.10.021. Epub 2011 Oct, 25. PMID:22044478 doi:10.1016/j.gene.2011.10.021
  2. Messori L, Merlino A. Ruthenium metalation of proteins: the X-ray structure of the complex formed between NAMI-A and hen egg white lysozyme. Dalton Trans. 2014 Mar 25;43(16):6128-31. doi: 10.1039/c3dt53582g. PMID:24553967 doi:http://dx.doi.org/10.1039/c3dt53582g

4ny5, resolution 1.85Å

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