1r8g

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(Difference between revisions)

Revision as of 23:48, 11 September 2015

Structure and function of YbdK

Structural highlights

1r8g is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	YBDK, B0581 ("Bacillus coli" Migula 1895)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GCS2_ECOLI] ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate.[HAMAP-Rule:MF_01609]^[1]

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

The Escherichia coli open reading frame YbdK encodes a member of a large bacterial protein family of unknown biological function. The sequences within this family are remotely related to the sequence of gamma-glutamate-cysteine ligase (gamma-GCS), an enzyme in the glutathione biosynthetic pathway. A gene encoding gamma-GCS in E. coli is already known. The 2.15 A resolution crystal structure of YbdK reveals an overall fold similar to that of glutamine synthetase (GS), a nitrogen metabolism enzyme that ligates glutamate and ammonia to yield glutamine. GS and gamma-GCS perform related chemical reactions and require ATP and Mg2+ for their activity. The Mg2+-dependent binding of ATP to YbdK was confirmed by fluorescence spectroscopy employing 2'(or 3')-O-(trinitrophenyl)adenosine 5'-triphosphate, and yielding a dissociation constant of 3 +/- 0.5 microM. The structure of YbdK contains a crevice that corresponds to the binding sites of ATP, Mg2+ and glutamate in GS. Many of the GS residues that coordinate the metal ions and interact with glutamic acid and the phosphoryl and ribosyl groups of ATP are also present in YbdK. GS amino acids that have been associated with ammonia binding have no obvious counterparts in YbdK, consistent with a substrate specificity that is different from that of GS. Ligase activity between glutamic acid and each of the twenty amino acid residues was tested on high performance liquid chromatography (HPLC) by following the hydrolysis of ATP to ADP. Catalysis was observed only with cysteine. A pyruvate kinase/lactic acid dehydrogenase coupled assay was used to rule out GS activity and to determine that YbdK exhibits gamma-GCS activity. The catalytic rate was found to be approximately 500-fold slower than that reported for authentic gamma-GCS.

YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays.,Lehmann C, Doseeva V, Pullalarevu S, Krajewski W, Howard A, Herzberg O Proteins. 2004 Aug 1;56(2):376-83. PMID:15211520^[2]

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

References

↑ Lehmann C, Doseeva V, Pullalarevu S, Krajewski W, Howard A, Herzberg O. YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays. Proteins. 2004 Aug 1;56(2):376-83. PMID:15211520 doi:10.1002/prot.20103
↑ Lehmann C, Doseeva V, Pullalarevu S, Krajewski W, Howard A, Herzberg O. YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays. Proteins. 2004 Aug 1;56(2):376-83. PMID:15211520 doi:10.1002/prot.20103

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r8g"

@@ Line 2: / Line 2: @@
 <StructureSection load='1r8g' size='340' side='right' caption='[[1r8g]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1r8g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R8G FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1r8g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R8G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R8G FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YBDK, B0581 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YBDK, B0581 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r8g OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r8g RCSB], [http://www.ebi.ac.uk/pdbsum/1r8g 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=1r8g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r8g OCA], [http://pdbe.org/1r8g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r8g RCSB], [http://www.ebi.ac.uk/pdbsum/1r8g PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAAL_ECOLI CAAL_ECOLI]] ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate.<ref>PMID:15211520</ref>
+[[http://www.uniprot.org/uniprot/GCS2_ECOLI GCS2_ECOLI]] ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity. However, because of the low catalytic rate, the question remains whether L-cysteine is the actual biological substrate.[HAMAP-Rule:MF_01609]<ref>PMID:15211520</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1r8g" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Bacillus coli migula 1895]]
 [[Category: Doseeva, V]]
 [[Category: Herzberg, O]]

1r8g

From Proteopedia

Revision as of 23:48, 11 September 2015

Structure and function of YbdK

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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