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.


4mzd

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:30, 1 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==High resolution crystal structure of the nisin leader peptidase NisP from Lactococcus lactis==
==High resolution crystal structure of the nisin leader peptidase NisP from Lactococcus lactis==
-
<StructureSection load='4mzd' size='340' side='right' caption='[[4mzd]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
+
<StructureSection load='4mzd' size='340' side='right'caption='[[4mzd]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4mzd]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MZD FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4mzd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis_subsp._lactis Lactococcus lactis subsp. lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MZD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MZD FirstGlance]. <br>
-
</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=4mzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mzd RCSB], [http://www.ebi.ac.uk/pdbsum/4mzd PDBsum]</span></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.1&#8491;</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=4mzd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mzd OCA], [https://pdbe.org/4mzd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mzd RCSB], [https://www.ebi.ac.uk/pdbsum/4mzd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mzd ProSAT]</span></td></tr>
</table>
</table>
-
<div style="background-color:#fffaf0;">
+
== Function ==
-
== Publication Abstract from PubMed ==
+
[https://www.uniprot.org/uniprot/NISP_LACLL NISP_LACLL] Cleaves the lantibiotic nisin precursor peptide.
-
Nisin is a widely used antibacterial lantibiotic polypeptide produced by Lactococcus lactis. NisP belongs to the subtilase family and functions in the last step of nisin maturation as the leader-peptide peptidase. Deletion of the nisP gene in LAC71 results in the production of a non-active precursor peptide with the leader peptide unremoved. Here, the 1.1 A resolution crystal structure of NisP is reported. The structure shows similarity to other subtilases, which can bind varying numbers of Ca atoms. However, no calcium was found in this NisP structure, and the predicted calcium-chelating residues were placed so as to not allow NisP to bind a calcium ion in this conformation. Interestingly, a short peptide corresponding to its own 635-647 sequence was found to bind to the active site of NisP. Biochemical assays and native mass-spectrometric analysis confirmed that NisP possesses an auto-cleavage site between residues Arg647 and Ser648. Further, it was shown that NisP mutated at the auto-cleavage site (R647P/S648P) had full catalytic activity for nisin leader-peptide cleavage, although the C-terminal region of NisP was no longer cleaved. Expressing this mutant in L. lactis LAC71 did not affect the production of nisin but did decrease the proliferation rate of the bacteria, suggesting the biological significance of the C-terminal auto-cleavage of NisP.
+
-
 
+
-
Structure of the nisin leader peptidase NisP revealing a C-terminal autocleavage activity.,Xu Y, Li X, Li R, Li S, Ni H, Wang H, Xu H, Zhou W, Saris PE, Yang W, Qiao M, Rao Z Acta Crystallogr D Biol Crystallogr. 2014 Jun;70(Pt 6):1499-505. doi:, 10.1107/S1399004714004234. Epub 2014 May 23. PMID:24914961<ref>PMID:24914961</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Li, X]]
+
[[Category: Lactococcus lactis subsp. lactis]]
-
[[Category: Rao, Z H]]
+
[[Category: Large Structures]]
-
[[Category: Xu, Y Y]]
+
[[Category: Li X]]
-
[[Category: Yang, W]]
+
[[Category: Rao ZH]]
-
[[Category: Alpha and beta protein]]
+
[[Category: Xu YY]]
-
[[Category: Hydrolase]]
+
[[Category: Yang W]]
-
[[Category: Serine protease]]
+
-
[[Category: Subtilisin-like]]
+

Current revision

High resolution crystal structure of the nisin leader peptidase NisP from Lactococcus lactis

PDB ID 4mzd

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4mzd"
Personal tools