4bhd - Revision history

OCA at 11:51, 20 December 2023

OCA — Wed, 20 Dec 2023 11:51:24 GMT

←Older revision		Revision as of 11:51, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='4bhd' size='340' side='right'caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>		<StructureSection load='4bhd' size='340' side='right'caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Atcc_43067 Atcc 43067~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHD FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>~~</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]] 2.83Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[4bhe\|4bhe]]~~</~~div~~></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [https://pdbe.org/4bhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [https://www.ebi.ac.uk/pdbsum/4bhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhd 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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [https://pdbe.org/4bhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [https://www.ebi.ac.uk/pdbsum/4bhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>	+	[https://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Atcc 43067]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Angelucci, F~~]]	+	[[Category: Methanocaldococcus jannaschii]]
-	[[Category: ~~Ilari, A~~]]	+	[[Category: Angelucci F]]
-	[[Category: ~~Saccoccia, F~~]]	+	[[Category: Ilari A]]
-	[[Category: ~~Transferase~~]]	+	[[Category: Saccoccia F]]

OCA at 07:13, 31 August 2022

OCA — Wed, 31 Aug 2022 07:13:55 GMT

←Older revision		Revision as of 07:13, 31 August 2022
Line 3:		Line 3:
	<StructureSection load='4bhd' size='340' side='right'caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>		<StructureSection load='4bhd' size='340' side='right'caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4BHD FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BHD FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bhe\|4bhe]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bhe\|4bhe]]</div></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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [~~http~~://pdbe.org/4bhd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4bhd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhd 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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [https://pdbe.org/4bhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [https://www.ebi.ac.uk/pdbsum/4bhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>	+	[[https://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 21:		Line 21:

	==See Also==		==See Also==
-	*[[Serine hydroxymethyltransferase\|Serine hydroxymethyltransferase]]	+	*[[Serine hydroxymethyltransferase 3D structures\|Serine hydroxymethyltransferase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 13:28, 13 March 2019

OCA — Wed, 13 Mar 2019 13:28:17 GMT

←Older revision		Revision as of 13:28, 13 March 2019
Line 1:		Line 1:

	==Methanococcus jannaschii serine hydroxymethyl-transferase, apo form==		==Methanococcus jannaschii serine hydroxymethyl-transferase, apo form==
-	<StructureSection load='4bhd' size='340' side='right' caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>	+	<StructureSection load='4bhd' size='340' side='right'caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BHD FirstGlance]. <br>		<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BHD FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4bhd" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4bhd" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Serine hydroxymethyltransferase\|Serine hydroxymethyltransferase]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Atcc 43067]]		[[Category: Atcc 43067]]
		+	[[Category: Large Structures]]
	[[Category: Angelucci, F]]		[[Category: Angelucci, F]]
	[[Category: Ilari, A]]		[[Category: Ilari, A]]
	[[Category: Saccoccia, F]]		[[Category: Saccoccia, F]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 18:33, 1 February 2017

OCA — Wed, 01 Feb 2017 18:33:36 GMT

←Older revision		Revision as of 18:33, 1 February 2017
Line 1:		Line 1:
		+
	==Methanococcus jannaschii serine hydroxymethyl-transferase, apo form==		==Methanococcus jannaschii serine hydroxymethyl-transferase, apo form==
	<StructureSection load='4bhd' size='340' side='right' caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>		<StructureSection load='4bhd' size='340' side='right' caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bhe\|4bhe]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bhe\|4bhe]]</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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [http://www.ebi.ac.uk/pdbsum/4bhd 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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [http://pdbe.org/4bhd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [http://www.ebi.ac.uk/pdbsum/4bhd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bhd ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
-		+	<div class="pdbe-citations 4bhd" style="background-color:#fffaf0;"></div>
-	==~~See Also==~~	+
-	*[[Serine hydroxymethyltransferase\|Serine hydroxymethyltransferase]]	+
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:27, 22 April 2015

OCA — Wed, 22 Apr 2015 06:27:11 GMT

←Older revision		Revision as of 06:27, 22 April 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>		[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Serine hydroxymethyltransferases (SHMTs) play an essential role in one-carbon unit metabolism and are employed in biomimetic reactions. We determined the crystal structure of free (apo) and PLP-bound (holo) SHMT from Methanocaldococcus jannaschii, the first from a hyperthermophile, from the archaea domain of life and that uses H4 MPT as a cofactor, at 2.83 and 3.0 A resolution, respectively. Idiosyncratic features were observed that are likely to contribute to structure stabilization. At the dimer interface, the C-terminal region folds in a unique fashion with respect to SHMTs from eubacteria and eukarya. At the active site, the conserved tyrosine does not make a cation-pi interaction with an arginine like that observed in all other SHMT structures, but establishes an amide-aromatic interaction with Asn257, at a different sequence position. This asparagine residue is conserved and occurs almost exclusively in (hyper)thermophile SHMTs. This led us to formulate the hypothesis that removal of frustrated interactions (such as the Arg-Tyr cation-pi interaction occurring in mesophile SHMTs) is an additional strategy of adaptation to high temperature. Both peculiar features may be tested by designing enzyme variants potentially endowed with improved stability for applications in biomimetic processes. (c) Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
		+
		+	The crystal structure of archaeal serine hydroxymethyltransferase reveals idiosyncratic features likely required to withstand high temperatures.,Angelucci F, Morea V, Angelaccio S, Saccoccia F, Contestabile R, Ilari A Proteins. 2014 Sep 26. doi: 10.1002/prot.24697. PMID:25257552<ref>PMID:25257552</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==

OCA at 16:18, 25 December 2014

OCA — Thu, 25 Dec 2014 16:18:15 GMT

←Older revision		Revision as of 16:18, 25 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4bhd\| PDB=4bhd \| SCENE= }}~~	+	==Methanococcus jannaschii serine hydroxymethyl-transferase, apo form==
-	===Methanococcus jannaschii serine hydroxymethyl-transferase, apo form===	+	<StructureSection load='4bhd' size='340' side='right' caption='[[4bhd]], [[Resolution\|resolution]] 2.83Å' scene=''>
-		+	== Structural highlights ==
-	==Function==	+	<table><tr><td colspan='2'>[[4bhd]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BHD FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4bhe\|4bhe]]</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=4bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bhd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bhd RCSB], [http://www.ebi.ac.uk/pdbsum/4bhd PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
	[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>		[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>

-	==~~About this Structure~~==	+	==See Also==
-	[[~~4bhd~~]] ~~is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA].~~	+	*[[Serine hydroxymethyltransferase\|Serine hydroxymethyltransferase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
-	[[Category: Angelucci, F.]]	+	</StructureSection>
-	[[Category: Ilari, A.]]	+	[[Category: Atcc 43067]]
-	[[Category: Saccoccia, F.]]	+	[[Category: Angelucci, F]]
		+	[[Category: Ilari, A]]
		+	[[Category: Saccoccia, F]]
	[[Category: Transferase]]		[[Category: Transferase]]

OCA at 09:58, 16 April 2014

OCA — Wed, 16 Apr 2014 09:58:22 GMT

←Older revision		Revision as of 09:58, 16 April 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4bhd\| PDB=4bhd \| SCENE= }}
		+	===Methanococcus jannaschii serine hydroxymethyl-transferase, apo form===

-	The ~~entry 4bhd~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/GLYA_METJA GLYA_METJA]] Catalyzes the reversible interconversion of serine and glycine with tetrahydromethanopterin (H4MPT) serving as the one-carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as the pteridine substrate is 450-fold less efficient than that of H4MPT. Also exhibits a pteridine-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine and L-threo-beta-phenylserine.<ref>PMID:12902326</ref>

-	~~Authors~~: ~~Saccoccia, F~~.~~, Angelucci, F~~.~~, Ilari, A~~.	+	==About this Structure==
		+	[[4bhd]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BHD OCA].

-	~~Description~~: ~~Methanococcus jannaschii serine hydroxymethyl-transferase~~, ~~apo form~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Angelucci, F.]]
		+	[[Category: Ilari, A.]]
		+	[[Category: Saccoccia, F.]]
		+	[[Category: Transferase]]

OCA at 03:15, 20 September 2013

OCA — Fri, 20 Sep 2013 03:15:36 GMT

←Older revision		Revision as of 03:15, 20 September 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4bhd is ON HOLD	+	The entry 4bhd is ON HOLD until Paper Publication

	Authors: Saccoccia, F., Angelucci, F., Ilari, A.		Authors: Saccoccia, F., Angelucci, F., Ilari, A.

	Description: Methanococcus jannaschii serine hydroxymethyl-transferase, apo form		Description: Methanococcus jannaschii serine hydroxymethyl-transferase, apo form

OCA: Protected "4bhd" [edit=sysop:move=sysop]

OCA — Wed, 17 Apr 2013 19:42:19 GMT

Protected "4bhd" [edit=sysop:move=sysop]

←Older revision

Revision as of 19:42, 17 April 2013

OCA: New page: '''Unreleased structure''' The entry 4bhd is ON HOLD Authors: Saccoccia, F., Angelucci, F., Ilari, A. Description: Methanococcus jannaschii serine hydroxymethyl-transferase, apo form

OCA — Wed, 17 Apr 2013 19:42:18 GMT

New page: '''Unreleased structure''' The entry 4bhd is ON HOLD Authors: Saccoccia, F., Angelucci, F., Ilari, A. Description: Methanococcus jannaschii serine hydroxymethyl-transferase, apo form

New page

'''Unreleased structure'''

The entry 4bhd is ON HOLD

Authors: Saccoccia, F., Angelucci, F., Ilari, A.

Description: Methanococcus jannaschii serine hydroxymethyl-transferase, apo form