1htq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1htq" [edit=sysop:move=sysop])
Current revision (04:49, 27 August 2024) (edit) (undo)
 
(11 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Large structure}}
 
-
[[Image:1htq.png|left|200px]]
 
-
<!--
+
==Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis==
-
The line below this paragraph, containing "STRUCTURE_1htq", creates the "Structure Box" on the page.
+
<StructureSection load='1htq' size='340' side='right'caption='[[1htq]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1htq]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HTQ FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;, 10 models</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=1htq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htq OCA], [https://pdbe.org/1htq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1htq RCSB], [https://www.ebi.ac.uk/pdbsum/1htq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1htq ProSAT]</span></td></tr>
-
{{STRUCTURE_1htq| PDB=1htq | SCENE= }}
+
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/GLN1B_MYCTU GLN1B_MYCTU] Involved in nitrogen metabolism via ammonium assimilation. Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia (PubMed:12819079, PubMed:7937767). Also able to use GTP (PubMed:7937767). D-glutamate is a poor substrate, and DL-glutamate shows about 50% of the standard specific activity (PubMed:7937767). Also plays a key role in controlling the ammonia levels within infected host cells and so contributes to the pathogens capacity to inhibit phagosome acidification and phagosome-lysosome fusion (PubMed:12819079, PubMed:7937767). Involved in cell wall biosynthesis via the production of the major component poly-L-glutamine (PLG) (PubMed:10618433, PubMed:7937767). PLG synthesis in the cell wall occurs only in nitrogen limiting conditions and on the contrary high nitrogen conditions inhibit PLG synthesis (Probable).<ref>PMID:10618433</ref> <ref>PMID:12819079</ref> <ref>PMID:7937767</ref> <ref>PMID:9278431</ref>
 +
== Evolutionary Conservation ==
 +
[[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/ht/1htq_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=1htq ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
The crystal structure of glutamine synthetase (GS) from Mycobacterium tuberculosis determined at 2.4 A resolution reveals citrate and AMP bound in the active site. The structure was refined with strict 24-fold noncrystallographic symmetry (NCS) constraints and has an R-factor of 22.7% and an R-free of 25.5%. Multicopy refinement using 10 atomic models and strict 24-fold NCS constraints further reduced the R-factor to 20.4% and the R-free to 23.2%. The multicopy model demonstrates the range of atomic displacements of catalytic and regulatory loops in glutamine synthesis, simulating loop motions. A comparison with loop positions in substrate complexes of GS from Salmonella typhimurium shows that the Asp50 and Glu327 loops close over the active site during catalysis. These loop closures are preceded by a conformational change of the Glu209 beta-strand upon metal ion or ATP binding that converts the enzyme from a relaxed to a taut state. We propose a model of the GS regulatory mechanism based on the loop motions in which adenylylation of the Tyr397 loop reverses the effect of metal ion binding, and regulates intermediate formation by preventing closure of the Glu327 loop.
-
===Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis===
+
Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation.,Gill HS, Pfluegl GM, Eisenberg D Biochemistry. 2002 Aug 6;41(31):9863-72. PMID:12146952<ref>PMID:12146952</ref>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_12146952}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1htq" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 12146952 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_12146952}}
+
-
 
+
-
==About this Structure==
+
-
[[1htq]] is a 24 chain structure of [[Glutamine Synthase]] with sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HTQ OCA].
+
==See Also==
==See Also==
-
*[[Glutamine Synthase|Glutamine Synthase]]
+
*[[Glutamine synthetase 3D structures|Glutamine synthetase 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:012146952</ref><references group="xtra"/>
+
__TOC__
-
[[Category: Glutamate--ammonia ligase]]
+
</StructureSection>
-
[[Category: Mycobacterium tuberculosis]]
+
[[Category: Large Structures]]
-
[[Category: Eisenberg, D.]]
+
-
[[Category: Gill, H S.]]
+
-
[[Category: Pfluegl, G M.]]
+
-
[[Category: TBSGC, TB Structural Genomics Consortium.]]
+
-
[[Category: Glutamine synthetase]]
+
-
[[Category: Ligase]]
+
-
[[Category: Multicopy refinement]]
+
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
-
[[Category: Protein structure initiative]]
+
[[Category: Eisenberg D]]
-
[[Category: Psi]]
+
[[Category: Gill HS]]
-
[[Category: Structural genomic]]
+
[[Category: Pfluegl GM]]
-
[[Category: Tb structural genomics consortium]]
+
-
[[Category: Tbsgc]]
+

Current revision

Multicopy crystallographic structure of a relaxed glutamine synthetase from Mycobacterium tuberculosis

PDB ID 1htq

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/1htq"
Personal tools