Difference between revisions of "Part:BBa K1998010"

Revision as of 09:47, 18 October 2016

HydG

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

Overview

This part is composed of the HydG gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of HydE, HydF, and HydG. Within several prokaryotic genomes HydE, HydF, and HydG are found in putative operons with [Fe] hydrogenase structural genes.

Biology & Literature

HydG is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. HydG breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that Hyd G cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. Hyd E and Hyd F are maturases also required for the assembly of an active hydrogenase [3]. The binding site in HydG can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].

Protein information

HydG
Mass: 63.74kDa
Sequence:
MSVPLQCNAGRLLAGQRPCGVRARLNRRVCVPVTAHGKASATREYAGDFLPGTTISHAWSVERETHHRYRNPAEWINEAA IHKALETSKADAQDAGRVREILAKAKEKAFVTEHAPVNAESKSEFVQGLTLEECATLINVDSNNVELMNEIFDTALAIKE RIYGNRVVLFAPLYIANHCMNTCTYCAFRSANKGMERSILTDDDLREEVAALQRQGHRRILALTGEHPKYTFDNFLHAVN VIASVKTEPEGSIRRINVEIPPLSVSDMRRLKNTDSVGTFVLFQETYHRDTFKVMHPSGPKSDFDFRVLTQDRAMRAGLD DVGIGALFGLYDYRYEVCAMLMHSEHLEREYNAGPHTISVPRMRPADGSELSIAPPYPVNDADFMKLVAVLRIAVPYTGM ILSTRESPEMRSALLKCGMSQMSAGSRTDVGAYHKDHTLSTEANLSKLAGQFTLQDERPTNEIVKWLMEEGYVPSWCTAC YRQGRTGEDFMNICKAGDIHDFCHPNSLLTLQEYLMDYADPDLRKKGEQVIAREMGPDASEPLSAQSRKRLERKMKQVLE GEHDVYL

References

[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of HydG, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.

[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.

[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.

[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme HydG. Biochemistry. 2013;52(48):8696-8707

@@ Line 1: / Line 1: @@
 __NOTOC__
 <partinfo>BBa_K1998010 short</partinfo>
-<!-- Add more about the biology of this part here
-===Usage and Biology===
 <!-- -->
@@ Line 16: / Line 12: @@
 <!-- -->
+===Overview===
 This part is composed of the HydG gene. All organisms with [Fe] hydrogenase and sequenced genomes contain homologues of HydE, HydF, and HydG. Within several prokaryotic genomes HydE, HydF, and HydG are found in putative operons with [Fe] hydrogenase structural genes.
+<br><br>
 <html><center><img src="https://static.igem.org/mediawiki/2016/8/81/T--Macquarie_Australia--HydrogenProduction.png" alt="HydrogenProduction" height="50%"width="75%"></center></html>
+===Biology & Literature===
+HydG is a radical S-adenosyl methionine (SAM) enzyme which catalyzes formation of a CO- and CN−-bound iron precursor to the H cluster, the cofactor on which [FeFe] hydrogenases are dependent on [1]. HydG breaks up the substrate tyrosine to yield both CO- and CN—ligands which act as precorsors during H-cluster assembly. It has been suggested that Hyd G cleaves the Cα–Cβ bond of tyrosine and p-cresol and dehydroglycine are formed as by-products [2]. Hyd E and Hyd F are maturases also required for the assembly of an active hydrogenase [3]. The binding site in HydG can accommodate either a [5Fe-5S] or a [4Fe-5S] cluster [4].
+===Protein information===
+HydG<br>
+Mass: 63.74kDa<br>
+Sequence: <br>
+MSVPLQCNAGRLLAGQRPCGVRARLNRRVCVPVTAHGKASATREYAGDFLPGTTISHAWSVERETHHRYRNPAEWINEAA
+IHKALETSKADAQDAGRVREILAKAKEKAFVTEHAPVNAESKSEFVQGLTLEECATLINVDSNNVELMNEIFDTALAIKE
+RIYGNRVVLFAPLYIANHCMNTCTYCAFRSANKGMERSILTDDDLREEVAALQRQGHRRILALTGEHPKYTFDNFLHAVN
+VIASVKTEPEGSIRRINVEIPPLSVSDMRRLKNTDSVGTFVLFQETYHRDTFKVMHPSGPKSDFDFRVLTQDRAMRAGLD
+DVGIGALFGLYDYRYEVCAMLMHSEHLEREYNAGPHTISVPRMRPADGSELSIAPPYPVNDADFMKLVAVLRIAVPYTGM
+ILSTRESPEMRSALLKCGMSQMSAGSRTDVGAYHKDHTLSTEANLSKLAGQFTLQDERPTNEIVKWLMEEGYVPSWCTAC
+YRQGRTGEDFMNICKAGDIHDFCHPNSLLTLQEYLMDYADPDLRKKGEQVIAREMGPDASEPLSAQSRKRLERKMKQVLE
+GEHDVYL
+<br>
+===References===
+[1] Dinis P, Suess D, Fox S, Harmer J, Driesener R, De La Paz L et al. X-ray crystallographic and EPR spectroscopic analysis of HydG, a maturase in [FeFe]-hydrogenase H-cluster assembly. Proceedings of the National Academy of Sciences. 2015;112(5):1362-1367.
+<br><br>
+[2] Pilet E, Nicolet Y, Mathevon C, Douki T, Fontecilla-Camps J, Fontecave M. The role of the maturase HydG in [FeFe]-hydrogenase active site synthesis and assembly. FEBS Letters. 2009;583(3):506-511.
+<br><br>
+[3] Posewitz M, King P, Smolinski S, Zhang L, Seibert M, Ghirardi M. Discovery of Two Novel Radical S-Adenosylmethionine Proteins Required for the Assembly of an Active [Fe] Hydrogenase. Journal of Biological Chemistry. 2004;279(24):25711-25720.
+<br><br>
+[4] Driesener R, Duffus B, Shepard E, Bruzas I, Duschene K, Coleman N et al. Biochemical and Kinetic Characterization of Radical S -Adenosyl- l -methionine Enzyme HydG. Biochemistry. 2013;52(48):8696-8707