1khd

From Proteopedia

(Difference between revisions)

Revision as of 07:31, 11 October 2017

Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum)

Structural highlights

1khd is a 4 chain structure with sequence from "bacillus_carotovorus"_jones_1901 "bacillus carotovorus" jones 1901. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1kgz
Gene:	trpD ("Bacillus carotovorus" Jones 1901)
Activity:	Anthranilate phosphoribosyltransferase, with EC number 2.4.2.18
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q8VP84_PECCA] Catalyzes the transfer of the phosphoribosyl group of 5-phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'-phosphoribosyl)-anthranilate (PRA).[HAMAP-Rule:MF_00211][SAAS:SAAS00083122]

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 structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum has been solved at 2.4 A in complex with Mn(2+)-pyrophosphate, and at 1.9 A without ligands. The enzyme structure has a novel phosphoribosyltransferase (PRT) fold and displays close homology to the structures of pyrimidine nucleoside phosphorylases. The enzyme is a homodimer with a monomer of 345 residues. Each monomer consists of two subdomains, alpha and alpha/beta, which form a cleft containing the active site. The nature of the active site is inferred from the trapped MnPPi complex and detailed knowledge of the active sites of nucleoside phosphorylases. With the anthranilate (An)PRT structure solved, the structures of all the enzymes required for tryptophan biosynthesis are now known.

The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum.,Kim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE FEBS Lett. 2002 Jul 17;523(1-3):239-46. PMID:12123839^[1]

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

References

↑ Kim C, Xuong NH, Edwards S, Madhusudan, Yee MC, Spraggon G, Mills SE. The crystal structure of anthranilate phosphoribosyltransferase from the enterobacterium Pectobacterium carotovorum. FEBS Lett. 2002 Jul 17;523(1-3):239-46. PMID:12123839

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/1khd"

@@ Line 1: / Line 1: @@
 ==Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum)==
 <StructureSection load='1khd' size='340' side='right' caption='[[1khd]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">trpD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=554 "Bacillus carotovorus" Jones 1901])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Anthranilate_phosphoribosyltransferase Anthranilate phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18 2.4.2.18] </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=1khd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khd OCA], [http://pdbe.org/1khd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1khd RCSB], [http://www.ebi.ac.uk/pdbsum/1khd 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=1khd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1khd OCA], [http://pdbe.org/1khd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1khd RCSB], [http://www.ebi.ac.uk/pdbsum/1khd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1khd ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1khd ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1khd" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Phosphoribosyltransferase|Phosphoribosyltransferase]]
 == References ==
 <references/>

1khd

From Proteopedia

Revision as of 07:31, 11 October 2017

Crystal Structure Analysis of the anthranilate phosphoribosyltransferase from Erwinia carotovora at 1.9 resolution (current name, Pectobacterium carotovorum)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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