3lmh

From Proteopedia

(Difference between revisions)

Revision as of 00:33, 5 August 2016

Crystal Structure of the Alpha-kinase Domain of Myosin Heavy Chain Kinase A Complex with ADP

Structural highlights

3lmh is a 2 chain structure with sequence from Atcc 11735. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
NonStd Res:
Related:	3lkm, 3lla, 3lmi
Gene:	DDB_G0291231, mhckA, mhkA, mnkA (ATCC 11735)
Activity:	[Myosin_heavy-chain_kinase [Myosin heavy-chain] kinase], with EC number 2.7.11.7
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MHCKA_DICDI] Phosphorylates threonine in the C-terminal tail region of myosin II heavy chain. This phosphorylation is critical in regulating the assembly and disassembly of myosin II filament. Requires autophosphorylation for activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Dictyostelium discoideum myosin II heavy chain kinase A (MHCK A) disrupts the assembly and cellular activity of bipolar filaments of myosin II by phosphorylating sites within its alpha-helical, coiled-coil tail. MHCK A is a member of the atypical alpha-kinase family of serine and threonine protein kinases and displays no sequence homology to typical eukaryotic protein kinases. We report the crystal structure of the alpha-kinase domain (A-CAT) of MHCK A. When crystallized in the presence of adenosine triphosphate (ATP), A-CAT contained adenosine monophosphate (AMP) at the active site. However, when crystallized in the presence of ATP and a peptide substrate, which does not appear in the structure, adenosine diphosphate (ADP) was found at the active site and an invariant aspartic acid residue (Asp(766)) at the active site was phosphorylated. The aspartylphosphate group was exposed to the solvent within an active-site pocket that might function as a docking site for substrates. Access to the aspartylphosphate was regulated by a conformational switch in a loop that bound to a magnesium ion (Mg(2+)), providing a mechanism that allows alpha-kinases to sense and respond to local changes in Mg(2+).

Crystal structure of the alpha-kinase domain of Dictyostelium myosin heavy chain kinase A.,Ye Q, Crawley SW, Yang Y, Cote GP, Jia Z Sci Signal. 2010 Mar 2;3(111):ra17. PMID:20197546^[1]

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

References

↑ Ye Q, Crawley SW, Yang Y, Cote GP, Jia Z. Crystal structure of the alpha-kinase domain of Dictyostelium myosin heavy chain kinase A. Sci Signal. 2010 Mar 2;3(111):ra17. PMID:20197546 doi:3/111/ra17

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3lmh"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the Alpha-kinase Domain of Myosin Heavy Chain Kinase A Complex with ADP==
 <StructureSection load='3lmh' size='340' side='right' caption='[[3lmh]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3lmh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Dictyostelium_discoideum Dictyostelium discoideum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LMH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3lmh]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_11735 Atcc 11735]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LMH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LMH FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lkm|3lkm]], [[3lla|3lla]], [[3lmi|3lmi]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0291231, mhckA, mhkA, mnkA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 Dictyostelium discoideum])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DDB_G0291231, mhckA, mhkA, mnkA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=44689 ATCC 11735])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/[Myosin_heavy-chain]_kinase [Myosin heavy-chain] kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.7 2.7.11.7] </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=3lmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lmh RCSB], [http://www.ebi.ac.uk/pdbsum/3lmh 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=3lmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lmh OCA], [http://pdbe.org/3lmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lmh RCSB], [http://www.ebi.ac.uk/pdbsum/3lmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lmh ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 20: / Line 21: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lmh ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 30: / Line 31: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 3lmh" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 37: / Line 39: @@
 __TOC__
 </StructureSection>
-[[Category: Dictyostelium discoideum]]
+[[Category: Atcc 11735]]
 [[Category: Jia, Z]]
 [[Category: Ye, Q]]

3lmh

From Proteopedia

Revision as of 00:33, 5 August 2016

Crystal Structure of the Alpha-kinase Domain of Myosin Heavy Chain Kinase A Complex with ADP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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