1gxb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:51, 9 May 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1gxb.gif|left|200px]]
 
-
{{Structure
+
==ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH PYROPHOSPHATE AND MAGNESIUM==
-
|PDB= 1gxb |SIZE=350|CAPTION= <scene name='initialview01'>1gxb</scene>, resolution 2.65&Aring;
+
<StructureSection load='1gxb' size='340' side='right'caption='[[1gxb]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
-
|SITE= <scene name='pdbsite=PP1:Mg+Binding+Site+For+Chain+D'>PP1</scene>
+
== Structural highlights ==
-
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=POP:PYROPHOSPHATE 2-'>POP</scene>
+
<table><tr><td colspan='2'>[[1gxb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GXB FirstGlance]. <br>
-
|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.18. 2.4.2.18.]
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</td></tr>
-
|GENE=
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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=1gxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gxb OCA], [https://pdbe.org/1gxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gxb RCSB], [https://www.ebi.ac.uk/pdbsum/1gxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gxb ProSAT]</span></td></tr>
-
 
+
</table>
-
'''ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH PYROPHOSPHATE AND MAGNESIUM'''
+
== Function ==
-
 
+
[https://www.uniprot.org/uniprot/TRPD_SACS2 TRPD_SACS2] 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]<ref>PMID:11298741</ref> <ref>PMID:16714288</ref>
-
 
+
== Evolutionary Conservation ==
-
==Overview==
+
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gx/1gxb_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<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/main_output.php?pdb_ID=1gxb ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.
The crystal structure of the dimeric anthranilate phosphoribosyltransferase (AnPRT) reveals a new category of phosphoribosyltransferases, designated as class III. The active site of this enzyme is located within the flexible hinge region of its two-domain structure. The pyrophosphate moiety of phosphoribosylpyrophosphate is co-ordinated by a metal ion and is bound by two conserved loop regions within this hinge region. With the structure of AnPRT available, structural analysis of all enzymatic activities of the tryptophan biosynthesis pathway is complete, thereby connecting the evolution of its enzyme members to the general development of metabolic processes. Its structure reveals it to have the same fold, topology, active site location and type of association as class II nucleoside phosphorylases. At the level of sequences, this relationship is mirrored by 13 structurally invariant residues common to both enzyme families. Taken together, these data imply common ancestry of enzymes catalysing reverse biological processes--the ribosylation and deribosylation of metabolic pathway intermediates. These relationships establish new links for enzymes involved in nucleotide and amino acid metabolism.
-
==About this Structure==
+
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry.,Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M EMBO J. 2002 Jul 1;21(13):3245-54. PMID:12093726<ref>PMID:12093726</ref>
-
1GXB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GXB OCA].
+
-
==Reference==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
Structural analysis of two enzymes catalysing reverse metabolic reactions implies common ancestry., Mayans O, Ivens A, Nissen LJ, Kirschner K, Wilmanns M, EMBO J. 2002 Jul 1;21(13):3245-54. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12093726 12093726]
+
</div>
-
[[Category: Single protein]]
+
<div class="pdbe-citations 1gxb" style="background-color:#fffaf0;"></div>
-
[[Category: Sulfolobus solfataricus]]
+
-
[[Category: Transferase]]
+
-
[[Category: Ivens, A.]]
+
-
[[Category: Kirschner, K.]]
+
-
[[Category: Mayans, O.]]
+
-
[[Category: Nissen, L J.]]
+
-
[[Category: Wilmanns, M.]]
+
-
[[Category: MG]]
+
-
[[Category: POP]]
+
-
[[Category: anthranilate phosphoribosyl transferase]]
+
-
[[Category: mg2+]]
+
-
[[Category: prpp]]
+
-
[[Category: pyrophosphate]]
+
-
[[Category: tryptophane biosynthesis]]
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:29:13 2008''
+
==See Also==
 +
*[[Phosphoribosyltransferase 3D structures|Phosphoribosyltransferase 3D structures]]
 +
== References ==
 +
<references/>
 +
__TOC__
 +
</StructureSection>
 +
[[Category: Large Structures]]
 +
[[Category: Saccharolobus solfataricus]]
 +
[[Category: Ivens A]]
 +
[[Category: Kirschner K]]
 +
[[Category: Mayans O]]
 +
[[Category: Nissen LJ]]
 +
[[Category: Wilmanns M]]

Current revision

ANTHRANILATE PHOSPHORIBOSYLTRANSFERASE IN COMPLEX WITH PYROPHOSPHATE AND MAGNESIUM

PDB ID 1gxb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1gxb"
Personal tools