2pkf: Difference between revisions

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<StructureSection load='2pkf' size='340' side='right'caption='[[2pkf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2pkf' size='340' side='right'caption='[[2pkf]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pkf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PKF FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pkf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PKF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PKF FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rka|1rka]], [[1bx4|1bx4]], [[1rkd|1rkd]], [[2pkk|2pkk]], [[2pkm|2pkm]], [[2pkn|2pkn]]</div></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]] 1.5&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Rv2202 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 "Bacillus tuberculosis" (Zopf 1883) Klein 1884])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Adenosine_kinase Adenosine kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.20 2.7.1.20] </span></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=2pkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkf OCA], [https://pdbe.org/2pkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pkf RCSB], [https://www.ebi.ac.uk/pdbsum/2pkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkf ProSAT]</span></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=2pkf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pkf OCA], [https://pdbe.org/2pkf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pkf RCSB], [https://www.ebi.ac.uk/pdbsum/2pkf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pkf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ADOK_MYCTU ADOK_MYCTU]] ATP dependent phosphorylation of adenosine to monophosphate derivatives (By similarity).  
[https://www.uniprot.org/uniprot/ADOK_MYCTU ADOK_MYCTU] ATP dependent phosphorylation of adenosine to monophosphate derivatives (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=2pkf 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=2pkf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adenosine kinase (ADK) catalyzes the phosphorylation of adenosine (Ado) to adenosine monophosphate (AMP). It is part of the purine salvage pathway that has been identified only in eukaryotes, with the single exception of Mycobacterium spp. Whereas it is not clear if Mycobacterium tuberculosis (Mtb) ADK is essential, it has been shown that the enzyme can selectively phosphorylate nucleoside analogs to produce products toxic to the cell. We have determined the crystal structure of Mtb ADK unliganded as well as ligand (Ado) bound at 1.5- and 1.9-A resolution, respectively. The structure of the binary complexes with the inhibitor 2-fluoroadenosine (F-Ado) bound and with the adenosine 5'-(beta,gamma-methylene)triphosphate (AMP-PCP) (non-hydrolyzable ATP analog) bound were also solved at 1.9-A resolution. These four structures indicate that Mtb ADK is a dimer formed by an extended beta sheet. The active site of the unliganded ADK is in an open conformation, and upon Ado binding a lid domain of the protein undergoes a large conformation change to close the active site. In the closed conformation, the lid forms direct interactions with the substrate and residues of the active site. Interestingly, AMP-PCP binding alone was not sufficient to produce the closed state of the enzyme. The binding mode of F-Ado was characterized to illustrate the role of additional non-bonding interactions in Mtb ADK compared with human ADK.
High resolution crystal structures of Mycobacterium tuberculosis adenosine kinase: insights into the mechanism and specificity of this novel prokaryotic enzyme.,Reddy MC, Palaninathan SK, Shetty ND, Owen JL, Watson MD, Sacchettini JC J Biol Chem. 2007 Sep 14;282(37):27334-42. Epub 2007 Jun 26. PMID:17597075<ref>PMID:17597075</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2pkf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Adenosine kinase 3D structures|Adenosine kinase 3D structures]]
*[[Adenosine kinase 3D structures|Adenosine kinase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Adenosine kinase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Owen, J L]]
[[Category: Palaninathan, S K]]
[[Category: Reddy, M C.M]]
[[Category: Sacchettini, J C]]
[[Category: Shetty, N D]]
[[Category: Structural genomic]]
[[Category: Watson, M D]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: PSI, Protein structure initiative]]
[[Category: Owen JL]]
[[Category: Tbsgc]]
[[Category: Palaninathan SK]]
[[Category: Transferase]]
[[Category: Reddy MCM]]
[[Category: Sacchettini JC]]
[[Category: Shetty ND]]
[[Category: Watson MD]]

Latest revision as of 12:10, 21 February 2024

Crystal structure of M tuberculosis Adenosine Kinase (apo)Crystal structure of M tuberculosis Adenosine Kinase (apo)

Structural highlights

2pkf is a 2 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ADOK_MYCTU ATP dependent phosphorylation of adenosine to monophosphate derivatives (By similarity).

Evolutionary Conservation

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

See Also

2pkf, resolution 1.50Å

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