4ml7

From Proteopedia

(Difference between revisions)

Revision as of 07:25, 11 August 2016

Crystal structure of Brucella abortus PliC in complex with human lysozyme

Structural highlights

4ml7 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Activity:	Lysozyme, with EC number 3.2.1.17
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[LYSC_HUMAN] Defects in LYZ are a cause of amyloidosis type 8 (AMYL8) [MIM:105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.^[1]

Function

[LYSC_HUMAN] 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.

Publication Abstract from PubMed

Lysozymes are the first line of defense for a diverse range of organisms that catalyze the degradation of bacterial peptidoglycan. Gram-negative bacteria produce proteinaceous lysozyme inhibitors to protect themselves from the action of lysozymes. To date, MliC or PliC (membrane-bound or periplasmic inhibitor of c-type lysozyme, respectively) has been found in various Gram-negative bacteria. Here, we report the crystal structures of Brucella abortus PliC and its complex with human c-type lysozyme. The complex structure demonstrates that the invariant loop of MliC/PliC plays a crucial role in the inhibition of lysozyme via its insertion into the active site cleft of the lysozyme, as previously observed in the complex structure of Pseudomonas aeruginosa MliC and chicken c-type lysozyme. We identified a new binding interface between a loop adjacent to the active site of human lysozyme and a loop carrying Glu112 of B. abortus PliC, the structure of which was disordered in P. aeruginosa MliC. Because MliC/PliC family members have been implicated as putative colonization or virulence factors, the structures and mechanism of action of MliC/PliC will be relevant to the control of bacterial growth in animal hosts.

Structural basis for the inhibition of human lysozyme by PliC from Brucella abortus.,Um SH, Kim JS, Kim K, Kim N, Cho HS, Ha NC Biochemistry. 2013 Dec 23;52(51):9385-93. doi: 10.1021/bi401241c. Epub 2013 Dec, 12. PMID:24308818^[2]

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

References

↑ Pepys MB, Hawkins PN, Booth DR, Vigushin DM, Tennent GA, Soutar AK, Totty N, Nguyen O, Blake CC, Terry CJ, et al.. Human lysozyme gene mutations cause hereditary systemic amyloidosis. Nature. 1993 Apr 8;362(6420):553-7. PMID:8464497 doi:http://dx.doi.org/10.1038/362553a0
↑ Um SH, Kim JS, Kim K, Kim N, Cho HS, Ha NC. Structural basis for the inhibition of human lysozyme by PliC from Brucella abortus. Biochemistry. 2013 Dec 23;52(51):9385-93. doi: 10.1021/bi401241c. Epub 2013 Dec, 12. PMID:24308818 doi:http://dx.doi.org/10.1021/bi401241c

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4ml7"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Brucella abortus PliC in complex with human lysozyme==
 <StructureSection load='4ml7' size='340' side='right' caption='[[4ml7]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4ml7]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ML7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ML7 FirstGlance]. <br>
 </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=4ml7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ml7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ml7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ml7 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=4ml7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ml7 OCA], [http://pdbe.org/4ml7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ml7 RCSB], [http://www.ebi.ac.uk/pdbsum/4ml7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ml7 ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ 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 4ml7" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4ml7

From Proteopedia

Revision as of 07:25, 11 August 2016

Crystal structure of Brucella abortus PliC in complex with human lysozyme

Structural highlights

Disease

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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