4j9j

From Proteopedia

(Difference between revisions)

Current revision

Structure of designed HisF

Structural highlights

4j9j is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HIS6_THEMA IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013]

Publication Abstract from PubMed

It has been postulated that the ubiquitous (betaalpha)8-barrel enzyme fold has evolved by duplication and fusion of an ancestral (betaalpha)4-half-barrel. We have previously reconstructed this process in the laboratory by fusing two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF). The resulting construct HisF-CC was stepwise stabilized to Sym1 and Sym2, which are extremely robust but catalytically inert proteins. Here, we report on the generation of a circular permutant of Sym2 and the establishment of a sugar isomerization reaction on its scaffold. Our results demonstrate that duplication and mutagenesis of (betaalpha)4-half-barrels can readily lead to a stable and catalytically active (betaalpha)8-barrel enzyme.

Establishing catalytic activity on an artificial (betaalpha)-barrel protein designed from identical half-barrels.,Sperl JM, Rohweder B, Rajendran C, Sterner R FEBS Lett. 2013 Jun 24. pii: S0014-5793(13)00469-9. doi:, 10.1016/j.febslet.2013.06.022. PMID:23806364^[1]

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

References

↑ Sperl JM, Rohweder B, Rajendran C, Sterner R. Establishing catalytic activity on an artificial (betaalpha)-barrel protein designed from identical half-barrels. FEBS Lett. 2013 Jun 24. pii: S0014-5793(13)00469-9. doi:, 10.1016/j.febslet.2013.06.022. PMID:23806364 doi:10.1016/j.febslet.2013.06.022

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4j9j"

Categories: Large Structures | Thermotoga maritima MSB8 | Rajendran C | Sperl J | Sterner R

@@ Line 1: / Line 1: @@
 ==Structure of designed HisF==
-<StructureSection load='4j9j' size='340' side='right' caption='[[4j9j]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
+<StructureSection load='4j9j' size='340' side='right'caption='[[4j9j]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4j9j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J9J FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4j9j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J9J FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">hisF, TM_1036 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</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]] 2.3&#8491;</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=4j9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9j OCA], [http://pdbe.org/4j9j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j9j RCSB], [http://www.ebi.ac.uk/pdbsum/4j9j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9j 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=4j9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j9j OCA], [https://pdbe.org/4j9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j9j RCSB], [https://www.ebi.ac.uk/pdbsum/4j9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j9j ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HIS6_THEMA HIS6_THEMA]] IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013]
+[https://www.uniprot.org/uniprot/HIS6_THEMA HIS6_THEMA] IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit.[HAMAP-Rule:MF_01013]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 4j9j" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[IGPS 3D structures|IGPS 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Thema]]
+[[Category: Large Structures]]
-[[Category: Rajendran, C]]
+[[Category: Thermotoga maritima MSB8]]
-[[Category: Sperl, J]]
+[[Category: Rajendran C]]
-[[Category: Sterner, R]]
+[[Category: Sperl J]]
-[[Category: Beta barrel]]
+[[Category: Sterner R]]
-[[Category: Lyase]]
-[[Category: Protein engineering]]

4j9j

From Proteopedia

Current revision

Structure of designed HisF

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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