This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4lt0

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:17, 5 August 2016

HEWL co-crystallized with Carboplatin in non-NaCl conditions: crystal 1 processed using the EVAL software package

Structural highlights

4lt0 is a 1 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4dd7, 4dd9, 4g4c, 4lt1, 4lt2, 4lt3
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

Carboplatin is a second-generation platinum anticancer agent used for the treatment of a variety of cancers. Previous X-ray crystallographic studies of carboplatin binding to histidine (in hen egg-white lysozyme; HEWL) showed the partial conversion of carboplatin to cisplatin owing to the high NaCl concentration used in the crystallization conditions. HEWL co-crystallizations with carboplatin in NaBr conditions have now been carried out to confirm whether carboplatin converts to the bromine form and whether this takes place in a similar way to the partial conversion of carboplatin to cisplatin observed previously in NaCl conditions. Here, it is reported that a partial chemical transformation takes place but to a transplatin form. Thus, to attempt to resolve purely carboplatin binding at histidine, this study utilized co-crystallization of HEWL with carboplatin without NaCl to eliminate the partial chemical conversion of carboplatin. Tetragonal HEWL crystals co-crystallized with carboplatin were successfully obtained in four different conditions, each at a different pH value. The structural results obtained show carboplatin bound to either one or both of the N atoms of His15 of HEWL, and this particular variation was dependent on the concentration of anions in the crystallization mixture and the elapsed time, as well as the pH used. The structural details of the bound carboplatin molecule also differed between them. Overall, the most detailed crystal structure showed the majority of the carboplatin atoms bound to the platinum centre; however, the four-carbon ring structure of the cyclobutanedicarboxylate moiety (CBDC) remained elusive. The potential impact of the results for the administration of carboplatin as an anticancer agent are described.

Carboplatin binding to histidine.,Tanley SW, Diederichs K, Kroon-Batenburg LM, Levy C, Schreurs AM, Helliwell JR Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1135-42. doi:, 10.1107/S2053230X14016161. Epub 2014 Aug 29. PMID:25195881^[2]

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

References

↑ 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
↑ Tanley SW, Diederichs K, Kroon-Batenburg LM, Levy C, Schreurs AM, Helliwell JR. Carboplatin binding to histidine. Acta Crystallogr F Struct Biol Commun. 2014 Sep 1;70(Pt 9):1135-42. doi:, 10.1107/S2053230X14016161. Epub 2014 Aug 29. PMID:25195881 doi:http://dx.doi.org/10.1107/S2053230X14016161

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4lt0"

@@ Line 1: / Line 1: @@
 ==HEWL co-crystallized with Carboplatin in non-NaCl conditions: crystal 1 processed using the EVAL software package==
 <StructureSection load='4lt0' size='340' side='right' caption='[[4lt0]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4dd7|4dd7]], [[4dd9|4dd9]], [[4g4c|4g4c]], [[4lt1|4lt1]], [[4lt2|4lt2]], [[4lt3|4lt3]]</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=4lt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lt0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lt0 RCSB], [http://www.ebi.ac.uk/pdbsum/4lt0 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=4lt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lt0 OCA], [http://pdbe.org/4lt0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lt0 RCSB], [http://www.ebi.ac.uk/pdbsum/4lt0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lt0 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4lt0" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4lt0

From Proteopedia

Revision as of 08:17, 5 August 2016

HEWL co-crystallized with Carboplatin in non-NaCl conditions: crystal 1 processed using the EVAL software package

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox