2lc0

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (19:13, 29 May 2024) (edit) (undo)
 
(7 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Rv0020c_Nter structure==
==Rv0020c_Nter structure==
-
<StructureSection load='2lc0' size='340' side='right' caption='[[2lc0]], [[NMR_Ensembles_of_Models | 30 NMR models]]' scene=''>
+
<StructureSection load='2lc0' size='340' side='right'caption='[[2lc0]]' scene=''>
== Structural highlights ==
== Structural highlights ==
-
[[2lc0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC0 OCA]. <br>
+
<table><tr><td colspan='2'>[[2lc0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis_H37Rv Mycobacterium tuberculosis H37Rv]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LC0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LC0 FirstGlance]. <br>
-
<b>[[Related_structure|Related:]]</b> [[2lc1|2lc1]]<br>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-
<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2lc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc0 OCA], [https://pdbe.org/2lc0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lc0 RCSB], [https://www.ebi.ac.uk/pdbsum/2lc0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lc0 ProSAT]</span></td></tr>
-
<b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2lc0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lc0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lc0 RCSB], [http://www.ebi.ac.uk/pdbsum/2lc0 PDBsum]</span><br>
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FHAA_MYCTU FHAA_MYCTU] Regulates cell growth and peptidoglycan synthesis by binding to MviN. May inhibit the late stages of peptidoglycan synthesis.<ref>PMID:22275220</ref>
 +
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
The protein Rv0020c from Mycobacterium tuberculosis, also called FhaA, is one of the major substrates of the essential Ser/Thr protein kinase (STPK) PknB. The protein is composed of three domains and is phosphorylated on a unique site in its N terminus. We solved the solution structure of both N- and C-terminal domains and demonstrated that the approximately 300 amino acids of the intermediate domain are not folded. We present evidence that the FHA, a phosphospecific binding domain, of Rv0020c does not interact with the phosphorylated catalytic domains of PknB, but with the phosphorylated juxtamembrane domain that links the catalytic domain to the mycobacterial membrane. We also demonstrated that the degree and the pattern of phosphorylation of this juxtamembrane domain modulates the affinity of the substrate (Rv0020c) toward its kinase (PknB).
The protein Rv0020c from Mycobacterium tuberculosis, also called FhaA, is one of the major substrates of the essential Ser/Thr protein kinase (STPK) PknB. The protein is composed of three domains and is phosphorylated on a unique site in its N terminus. We solved the solution structure of both N- and C-terminal domains and demonstrated that the approximately 300 amino acids of the intermediate domain are not folded. We present evidence that the FHA, a phosphospecific binding domain, of Rv0020c does not interact with the phosphorylated catalytic domains of PknB, but with the phosphorylated juxtamembrane domain that links the catalytic domain to the mycobacterial membrane. We also demonstrated that the degree and the pattern of phosphorylation of this juxtamembrane domain modulates the affinity of the substrate (Rv0020c) toward its kinase (PknB).
Line 11: Line 15:
Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase.,Roumestand C, Leiba J, Galophe N, Margeat E, Padilla A, Bessin Y, Barthe P, Molle V, Cohen-Gonsaud M Structure. 2011 Oct 12;19(10):1525-34. PMID:22000520<ref>PMID:22000520</ref>
Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase.,Roumestand C, Leiba J, Galophe N, Margeat E, Padilla A, Bessin Y, Barthe P, Molle V, Cohen-Gonsaud M Structure. 2011 Oct 12;19(10):1525-34. PMID:22000520<ref>PMID:22000520</ref>
-
From MEDLINE®/PubMed®, 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 class="pdbe-citations 2lc0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Mycobacterium tuberculosis]]
+
[[Category: Large Structures]]
-
[[Category: Barthe, P P.]]
+
[[Category: Mycobacterium tuberculosis H37Rv]]
-
[[Category: Cohen-Gonsaud, M M.]]
+
[[Category: Barthe PP]]
-
[[Category: Roumestand, C.]]
+
[[Category: Cohen-Gonsaud MM]]
-
[[Category: Fhaa]]
+
[[Category: Roumestand C]]
-
[[Category: Kinase substrate]]
+
-
[[Category: Protein binding]]
+

Current revision

Rv0020c_Nter structure

PDB ID 2lc0

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools