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==Crystal structure of Trp332Ala mutant YwfE, an L-amino acid ligase, with bound ADP-Mg-Ala==
==Crystal structure of Trp332Ala mutant YwfE, an L-amino acid ligase, with bound ADP-Mg-Ala==
<StructureSection load='3wo1' size='340' side='right' caption='[[3wo1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='3wo1' size='340' side='right'caption='[[3wo1]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3wo1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WO1 OCA]. <br>
<table><tr><td colspan='2'>[[3wo1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WO1 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vmm|3vmm]], [[3wnz|3wnz]], [[3wo0|3wo0]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></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=3wo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wo1 OCA], [https://pdbe.org/3wo1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wo1 RCSB], [https://www.ebi.ac.uk/pdbsum/3wo1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wo1 ProSAT]</span></td></tr>
<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=3wo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wo1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wo1 RCSB], [http://www.ebi.ac.uk/pdbsum/3wo1 PDBsum]</span></td></tr>
</table>
<table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/BACD_BACSU BACD_BACSU] Catalyzes the formation of alpha-dipeptides from various L-amino acids in the presence of ATP. Has a broad substrate specificity. Does not accept lysine, arginine, glutamate, aspartate and proline as a substrate. Probably catalyzes the ligation of L-alanine and L-anticapsin to produce the final bacilysin antibiotic.
== Publication Abstract from PubMed ==
l-Amino acid ligase (Lal) catalyzes the formation of a dipeptide from two l-amino acids in an ATP-dependent manner and belongs to the ATP-grasp superfamily. Bacillus subtilis YwfE, the first identified Lal, produces the dipeptide antibiotic bacilysin, which consists of l-Ala and l-anticapsin. Its substrate specificity is restricted to smaller amino acids such as l-Ala for the N-terminal end of the dipeptide, whereas a wide range of hydrophobic amino acids including l-Phe and l-Met are recognized for the C-terminal end in vitro. We determined the crystal structures of YwfE with bound ADP-Mg(2+)-Pi and ADP-Mg(2+)-l-Ala at 1.9 and 2.0 A resolutions, respectively. On the basis of these structures, we generated point mutants of residues that are considered to participate in the recognition of l-Ala and measured their ATPase activity. The conserved Arg328 is suggested to be a crucial residue for l-Ala recognition and catalysis. The mutation of Trp332 to Ala caused the enzyme to hydrolyze ATP, even in the absence of l-Ala, and the structure of this mutant protein appeared to show a cavity in the N-terminal substrate-binding pocket. These results suggest that Trp332 plays a key role in restricting the substrate specificity to smaller amino acids such as l-Ala. Moreover, Trp332 mutants can alter the substrate specificity and activity depending on the size and shape of substituted amino acids. These observations provide sufficient scope for the rational design of Lal to produce desirable dipeptides. We propose that the positioning of the conserved Arg residue in Lal is important for enantioselective recognition of l-amino acids.
 
Single Mutation Alters the Substrate Specificity of l-Amino Acid Ligase.,Tsuda T, Asami M, Koguchi Y, Kojima S Biochemistry. 2014 Apr 29;53(16):2650-60. doi: 10.1021/bi500292b. Epub 2014 Apr, 17. PMID:24702628<ref>PMID:24702628</ref>
 
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: L-amino-acid alpha-ligase]]
[[Category: Bacillus subtilis subsp. subtilis str. 168]]
[[Category: Kojima, S.]]
[[Category: Large Structures]]
[[Category: Tsuda, T.]]
[[Category: Kojima S]]
[[Category: Atp binding]]
[[Category: Tsuda T]]
[[Category: Atp-grasp fold]]
[[Category: Ligase]]

Latest revision as of 08:46, 20 March 2024

Crystal structure of Trp332Ala mutant YwfE, an L-amino acid ligase, with bound ADP-Mg-Ala

3wo1, resolution 2.30Å

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