4jx9

From Proteopedia

(Difference between revisions)

Revision as of 07:17, 23 December 2016

Crystal structure of the complex of peptidyl t-RNA hydrolase from Acinetobacter baumannii with uridine at 1.4A resolution

Structural highlights

4jx9 is a 1 chain structure with sequence from Acinetobacter baumannii 19606. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4iko, 4jwk, 4jy7, 4hoy, 4fot, 4fop
Gene:	pth, HMPREF0010_01329 (Acinetobacter baumannii 19606)
Activity:	Aminoacyl-tRNA hydrolase, with EC number 3.1.1.29
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[D0C9L6_ACIBA] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).[HAMAP-Rule:MF_00083]

Publication Abstract from PubMed

The incidences of infections caused by an aerobic Gram-negative bacterium, Acinetobacter baumannii are very common in hospital environments. It usually causes soft tissue infections including urinary tract infections and pneumonia. It is difficult to treat due to acquired resistance to available antibiotics is well known. In order to design specific inhibitors against one of the important enzymes, peptidyl-tRNA hydrolase from Acinetobacter baumannii, we have determined its three-dimensional structure. Peptidyl-tRNA hydrolase (AbPth) is involved in recycling of peptidyl-tRNAs which are produced in the cell as a result of premature termination of translation process. We have also determined the structures of two complexes of AbPth with cytidine and uridine. AbPth was cloned, expressed and crystallized in unbound and in two bound states with cytidine and uridine. The binding studies carried out using fluorescence spectroscopic and surface plasmon resonance techniques revealed that both cytidine and uridine bound to AbPth at nanomolar concentrations. The structure determinations of the complexes revealed that both ligands were located in the active site cleft of AbPth. The introduction of ligands to AbPth caused a significant widening of the entrance gate to the active site region and in the process of binding, it expelled several water molecules from the active site. As a result of interactions with protein atoms, the ligands caused conformational changes in several residues to attain the induced tight fittings. Such a binding capability of this protein makes it a versatile molecule for hydrolysis of peptidyl-tRNAs having variable peptide sequences. These are the first studies that revealed the mode of inhibitor binding in Peptidyl-tRNA hydrolases which will facilitate the structure based ligand design.

The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii.,Kaushik S, Singh N, Yamini S, Singh A, Sinha M, Arora A, Kaur P, Sharma S, Singh TP PLoS One. 2013 Jul 3;8(7):e67547. doi: 10.1371/journal.pone.0067547. Print 2013. PMID:23844024^[1]

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

References

↑ Kaushik S, Singh N, Yamini S, Singh A, Sinha M, Arora A, Kaur P, Sharma S, Singh TP. The Mode of Inhibitor Binding to Peptidyl-tRNA Hydrolase: Binding Studies and Structure Determination of Unbound and Bound Peptidyl-tRNA Hydrolase from Acinetobacter baumannii. PLoS One. 2013 Jul 3;8(7):e67547. doi: 10.1371/journal.pone.0067547. Print 2013. PMID:23844024 doi:10.1371/journal.pone.0067547

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/4jx9"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the complex of peptidyl t-RNA hydrolase from Acinetobacter baumannii with uridine at 1.4A resolution==
 <StructureSection load='4jx9' size='340' side='right' caption='[[4jx9]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4jx9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii_atcc_19606_=_cip_70.34 Acinetobacter baumannii atcc 19606 = cip 70.34]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JX9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4jx9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acinetobacter_baumannii_19606 Acinetobacter baumannii 19606]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JX9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4JX9 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=URI:URIDINE'>URI</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4iko|4iko]], [[4jwk|4jwk]], [[4jy7|4jy7]], [[4hoy|4hoy]], [[4fot|4fot]], [[4fop|4fop]]</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pth, HMPREF0010_01329 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=575584 Acinetobacter baumannii ATCC 19606 = CIP 70.34])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pth, HMPREF0010_01329 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=575584 Acinetobacter baumannii 19606])</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aminoacyl-tRNA_hydrolase Aminoacyl-tRNA hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.29 3.1.1.29] </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=4jx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jx9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4jx9 RCSB], [http://www.ebi.ac.uk/pdbsum/4jx9 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=4jx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4jx9 OCA], [http://pdbe.org/4jx9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4jx9 RCSB], [http://www.ebi.ac.uk/pdbsum/4jx9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4jx9 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/D0C9L6_ACIBA D0C9L6_ACIBA]] The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis (By similarity).[HAMAP-Rule:MF_00083]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 17: / Line 20: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4jx9" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 24: / Line 28: @@
 __TOC__
 </StructureSection>
-[[Category: Acinetobacter baumannii atcc 19606 = cip 70 34]]
+[[Category: Acinetobacter baumannii 19606]]
 [[Category: Aminoacyl-tRNA hydrolase]]
 [[Category: Kaur, P]]

4jx9

From Proteopedia

Revision as of 07:17, 23 December 2016

Crystal structure of the complex of peptidyl t-RNA hydrolase from Acinetobacter baumannii with uridine at 1.4A resolution

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox