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==The regulatory subunit of aspartate kinase from Mycobacterium tuberculosis==
==The regulatory subunit of aspartate kinase from Mycobacterium tuberculosis==
<StructureSection load='4go5' size='340' side='right' caption='[[4go5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
<StructureSection load='4go5' size='340' side='right'caption='[[4go5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4go5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GO5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4go5]] is a 1 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=4GO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GO5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4go7|4go7]]</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]] 2.6&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ask, Rv3709c, MT3812, MTV025.057c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1773 Mycobacterium tuberculosis])</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=4go5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4go5 OCA], [https://pdbe.org/4go5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4go5 RCSB], [https://www.ebi.ac.uk/pdbsum/4go5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4go5 ProSAT]</span></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aspartate_kinase Aspartate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.2.4 2.7.2.4] </span></td></tr>
</table>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4go5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4go5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4go5 RCSB], [http://www.ebi.ac.uk/pdbsum/4go5 PDBsum]</span></td></tr>
== Function ==
<table>
[https://www.uniprot.org/uniprot/AK_MYCTU AK_MYCTU] Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The aspartate kinase (AK) from Mycobacterium tuberculosis (Mtb) catalyzes the biosynthesis of aspartate family amino acids, including lysine, threonine, isoleucine and methionine. We determined the crystal structures of the regulatory subunit of aspartate kinase from Mtb alone (referred to as MtbAKbeta) and in complex with threonine (referred to as MtbAKbeta-Thr) at resolutions of 2.6 A and 2.0 A, respectively. MtbAKbeta is composed of two perpendicular non-equivalent ACT domains [aspartate kinase, chorismate mutase, and TyrA (prephenate dehydrogenase)] per monomer. Each ACT domain contains two alpha helices and four antiparallel beta strands. The structure of MtbAKbeta shares high similarity with the regulatory subunit of the aspartate kinase from Corynebacterium glutamicum (referred to as CgAKbeta), suggesting similar regulatory mechanisms. Biochemical assays in our study showed that MtbAK is inhibited by threonine. Based on crystal structure analysis, we discuss the regulatory mechanism of MtbAK.
 
Structural view of the regulatory subunit of aspartate kinase from Mycobacterium tuberculosis.,Yang Q, Yu K, Yan L, Li Y, Chen C, Li X Protein Cell. 2011 Sep;2(9):745-54. Epub 2011 Oct 6. PMID:21976064<ref>PMID:21976064</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: Aspartate kinase]]
[[Category: Large Structures]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Li, X.]]
[[Category: Li X]]
[[Category: Yang, Q.]]
[[Category: Yang Q]]
[[Category: Transferase]]

Latest revision as of 14:33, 1 March 2024

The regulatory subunit of aspartate kinase from Mycobacterium tuberculosisThe regulatory subunit of aspartate kinase from Mycobacterium tuberculosis

Structural highlights

4go5 is a 1 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 2.6Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AK_MYCTU Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids lysine, threonine, isoleucine and methionine.

4go5, resolution 2.60Å

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