4mir: Difference between revisions
New page: '''Unreleased structure''' The entry 4mir is ON HOLD Authors: Ha, N.C., Um, S.H., Kim, J.S. Description: The structure of Brucella abortus PliC in the hexagonal crystal form |
No edit summary |
||
| (7 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
The | ==The structure of Brucella abortus PliC in the hexagonal crystal form== | ||
<StructureSection load='4mir' size='340' side='right'caption='[[4mir]], [[Resolution|resolution]] 2.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4mir]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Brucella_abortus_bv._1_str._9-941 Brucella abortus bv. 1 str. 9-941]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MIR 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]] 2.4Å</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=4mir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mir OCA], [https://pdbe.org/4mir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mir RCSB], [https://www.ebi.ac.uk/pdbsum/4mir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mir ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q57ES7_BRUAB Q57ES7_BRUAB] | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:24308818</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4mir" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Brucella abortus bv. 1 str. 9-941]] | |||
[[Category: Large Structures]] | |||
[[Category: Ha NC]] | |||
[[Category: Kim JS]] | |||
[[Category: Um SH]] | |||
Latest revision as of 11:26, 9 October 2024
The structure of Brucella abortus PliC in the hexagonal crystal formThe structure of Brucella abortus PliC in the hexagonal crystal form
Structural highlights
FunctionPublication Abstract from PubMedLysozymes 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||